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Classification and Comparative Enzymology of the Cholinesterases and Methods for their Determination

  • Chapter
Cholinesterases and Anticholinesterase Agents

Part of the book series: Handbook of Experimental Pharmacology ((HEP,volume 15))

Abstract

Cholinesterases (ChE’s) are defined simply as enzymes which catalyze the hydrolysis of choline esters. There has been considerable discussion during the last 20 years on the specificity of these enzymes, their role in physiological systems, and the pharmacological importance of cholinesterase inhibitors. Everybody taking part in this discussion on the biochemical level will probably agree with the following; There are enzymes present in the animal body which split acetylcholine (ACh) and other choline esters at a very high rate. None of these enzymes so far studied splits only esters of choline; non-choline esters are also hydrolyzed, but at a lower rate. The specificity of cholinesterases therefore is not absolute, and “true” cholinesterases do not exist as far as the specificity is concerned.

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Literature

  • Abdon, N.-O., and B. UvnÄs: A step-photometric method for determining the activity of acetylcholine esterase in blood plasma. Skand. Arch. Physiol. 76, 1–14 (1937).

    Article  CAS  Google Scholar 

  • Adams, D. H.: The specificity of the human erythrocyte cholinesterase. Biochim. biophys. Acta 3, 1–14 (1949).

    CAS  Google Scholar 

  • Adams, D. H. and R. H. S. Thompson: The selective inhibition of cholinesterases. Biochem. J. 42, 170–175 (1948).

    Google Scholar 

  • Adams, D. H. and V. P. Whittaker: The cholinesterases of human blood. I. The specificity of the plasma enzyme and its relation to the erythrocyte cholinesterase. Biochim. biophys. Acta 3, 358 to 366 (1949).

    Google Scholar 

  • Adams, D. H. and V. P. Whittaker: The cholinesterases of human blood. II. The forces acting between enzyme and substrate. Biochim. biophys. Acta 4, 543–558 (1950).

    CAS  Google Scholar 

  • Adler, P., I. Gal u. L. Végh: Der Einfluß von Lokalanästhetika verschiedener Struktur auf die Cholinesterase-Aktivität im menschlichen Serum. Z. Vitamin-, Hormon-u. Ferment-forsch. 3, 236–243 (1949).

    Google Scholar 

  • Alcalde, J. M. O.: Serum cholinesterase determination in the differential diagnosis of jaundice. J. Lab. clin. Med. 36, 391–398 (1950).

    CAS  PubMed  Google Scholar 

  • Aldridge, W. N.: The differentiation of true and pseudo cholinesterase by organophosphorus compounds. Biochem. J. 53, 62–67 (1953a).

    CAS  PubMed  Google Scholar 

  • Aldridge, W. N.: Serum esterases. I. Two types of esterase (A and B) hydrolysing p-nitrophenyl acetate, propionate and butyrate, and a method for their determination. Biochem. J. 53, 110–117 (1953 b).

    Google Scholar 

  • Aldridge, W. N. and D. R. Davies: Determination of cholinesterase activity in human blood. Brit. med. J. 1952 I, 945–947.

    Article  Google Scholar 

  • Aldridge, W. N. and D. R. Davies and M. K. Johnsson: Cholinesterase, succinic dehydrogenase, nucleic acids, esterase and glutathione reductase in sub-cellular fractions from rat brain. Biochem. J. 73, 270–276 (1959).

    CAS  PubMed  Google Scholar 

  • Alles, G. A., and R. C. Hawes: Cholinesterases in the blood of man J biol. Chem. 133, 375–390 (1940).

    CAS  Google Scholar 

  • Ammon, R.: Die fermentative Spaltung des Acetylcholins. Pflügers Arch. ges. Physiol. 233, 486–491 (1933).

    CAS  Google Scholar 

  • U. F. J. Zapp: Eine einfache klinisch-chemische Methode zum Nachweis der Cholinesterase im Serum. Klin. Wschr. 33, 759–762 (1955).

    Article  PubMed  Google Scholar 

  • Arellano Celis, H., and J. G. Villasante: The practical usefulness of the method of Morand and Laborit for the determination of cholinesterase activity in exploration of liver function (Spanish). Rev. clin. esp. 50, 22–24 (1953).

    CAS  Google Scholar 

  • Arnold, A., A. E. Soria and F. K. Kirchner: A new anticholinesterase oxamide. Proc. Soc. exp. Biol. (N. Y.) 87, 393–394 (1954).

    Article  CAS  Google Scholar 

  • Arragon, G., et E. Sala: Recherches sur la cholinesterase. II. Extraction à partir des hématies. Bull. Soc. Chim. biol. (Paris) 30, 51–54 (1948).

    CAS  Google Scholar 

  • Arvy, L.: Les techniques actuelles d’histoenzymologie. Les estérases carboxyliques. Biol. méd. (Paris) 47, 12–160 (1958).

    CAS  Google Scholar 

  • Aouustinsson, K.-B.: Studies on blood choline esterase. Ark. Kemi, Miner. Geol. 18 A, No. 24, 1–16 (1944).

    Google Scholar 

  • Aouustinsson, K.-B.: Cholinesterases in some marine invertebrates. Acta physiol. scand. 11, 141–150 (1946a).

    Article  Google Scholar 

  • Aouustinsson, K.-B.: Studies on the specificity of choline esterase in Helix pomatia. Biochem. J. 40, 343–349 (1946 b).

    Google Scholar 

  • Aouustinsson, K.-B.: Cholinesterases. A study in comparative enzymology. Acta physiol. scand. 15, Suppl. 52, 1–182 (1948).

    Google Scholar 

  • Aouustinsson, K.-B.: Substrate concentration and specificity of choline ester splitting enzymes. Arch. Biochem. 23, 111–126 (1949).

    Google Scholar 

  • Aouustinsson, K.-B.: Acetylcholine-esterase and cholinesterase. In; J. B. SUMNER and K. MYRBACK, Eds., The Enzymes, vol. I, Part 1, 443–472. New York. Academic Press 1950a.

    Google Scholar 

  • Aouustinsson, K.-B.: The hydrolysis of non-choline esters by acetylcholine-esterase from human erythrocytes. Acta chem. scand. 4, 948–956 (1950b).

    Article  Google Scholar 

  • Aouustinsson, K.-B. J. B. Sumner and K. Myrbackl: Comparison between the acetylcholinesterases of Helix blood and cobra venom. I. The hydrolysis of acetylcholine and its inhibition by various compounds. Acta chem. scand. 5, 699–711 (1951 a).

    Google Scholar 

  • Aouustinsson, K.-B.: Comparison between the acetylcholinesterases of Helix blood and cobra venom. II. The hydrolysis of certain choline and non-choline esters. Acta chem. scand. 5, 712–723 (1951 b).

    Google Scholar 

  • Aouustinsson, K.-B.: Protection of cholinesterases by procaine against inactivation by Tabun in vitro. Acta physiol. scand. 27, 10–17 (1952).

    Article  Google Scholar 

  • Aouustinsson, K.-B.: Neuere Ergebnisse auf dem Gebiet der Cholinesterases und ihre Bedeutung für Pharmakologie und Toxikologie. Arzneimittel-Forsch. 4, 242–249 (1954).

    Google Scholar 

  • Aouustinsson, K.-B.: The normal variation of human blood cholinesterase activity. Acta physiol. scand. 35, 40–52 (1955 a).

    Google Scholar 

  • Aouustinsson, K.-B.: A titrimetric method for the determination of plasma and red blood cell cholinesterase activity using thiocholine esters as substrates. Scand. J. clin. Lab. Invest. 7, 284–290 (1955b).

    Article  Google Scholar 

  • Aouustinsson, K.-B.: The electric organs and their cholinesterase activity. Pubbl. Staz. zool. Napoli 27, 189–198 (1955 c).

    Google Scholar 

  • Aouustinsson, K.-B.: Assay methods for cholinesterases. Meth. biochem. Anal. 5, 1–63 (1957).

    Google Scholar 

  • Aouustinsson, K.-B.: Electrophoretic separation and classification of blood plasma esterases. Nature (Lond.) 181, 1786–1789 (1958a).

    Article  Google Scholar 

  • Aouustinsson, K.-B.: A new type of cholinesterase in sow’s milk. Acta chem. scand. 12, 1150–1152 (1958b).

    Article  Google Scholar 

  • Aouustinsson, K.-B.: Electrophoresis studies on blood plasma esterases. I. Mammalian plasmata. Acta chem. scand. 13, 571–592 (1959a).

    Article  Google Scholar 

  • Aouustinsson, K.-B.: Electrophoresis studies on blood plasma esterases. II. Avian, reptilian, amphibian and piscine plasmata. Acta chem. scand. 13, 1081–1096 (1959b).

    Article  Google Scholar 

  • Aouustinsson, K.-B.: Electrophoresis studies on blood plasma esterases. III. Conclusions. Acta chem. scand. 13, 1097–1105 (1959c).

    Article  Google Scholar 

  • Aouustinsson, K.-B.: Butyryl-and propionylcholinesterases and related types of eserine-sensitive esterases. In; P. D. BOYER, H. LARDY and K. MYRBACK, Eds., The Enzymes, 2nd ed., vol. 4, 521–540. New York. Academic Press 1960.

    Google Scholar 

  • Aouustinsson, K.-B. and G. Heimbürger: The determination of cholinesterase activity in blood samples absorbed on filter paper. Acta physiol. scand. 30, 45–54 (1953).

    Article  Google Scholar 

  • Aouustinsson, K.-B. and T. IsACasEN: The enzymic hydrolysis of the ß-methyl derivatives of acetylcholine and acetylthiocholine. Acta chem. scand. 11, 750–751 (1957).

    Article  Google Scholar 

  • Aouustinsson, K.-B. and D. Nachmansohn: Distinction between acetylcholine-esterase and other choline ester-splitting enzymes. Science 110, 98–99 (1949).

    Article  Google Scholar 

  • Aouustinsson, K.-B. and D. Nachmansohn and B. OLSsox: Esterases in the milk and blood plasma of swine. 1. Substrate specificity and electrophoresis studies. Biochem. J. 71, 477–484 (1959).

    Google Scholar 

  • Austin, L., and W. K. Berry: Two selective inhibitors of cholinesterase. Biochem. J. 54, 695–700 (1953).

    CAS  PubMed  Google Scholar 

  • Babers, F. H., and J. J. Pratt Jr.: A comparison of the cholinesterase in the heads of the house fly, the cockroach, and the honey bee. Physiol. Zool. 24, 127–131 (1951).

    CAS  PubMed  Google Scholar 

  • Bader, R., F. Schutz and M. Stacey: A crystalline serum mucoprotein with high choline-esterase activity. Nature (Lond.) 154, 183 (1944).

    Article  CAS  Google Scholar 

  • Barnes, J. M., W. J. Hayes and K. Kay: Control of health hazards likely to arise from the use of organophosphorus insecticides in vector control. Annex. Blood-holinesterase determinations. Bull. Wld Hlth Org. 16, 41–61 (1957).

    CAS  Google Scholar 

  • Barrnett, R. J.: The distribution of esterolytic activity in the tissues of the albino rat as demonstrated with indoxyl acetate. Anat. Rec. 114, 577–600 (1952).

    Article  CAS  PubMed  Google Scholar 

  • Bastide, P.: Contribution à l’étude de la richesse enzymatique des humeurs et des tissus chez les Helix. Clermont-Ferrand Imp. G. de Bussac 1954.

    Google Scholar 

  • Bastide, P. et G. Dastugue: Sur l’hydrolyse enzymatique de quelques anesthésiques locaux (procaine et autres esters para-aminobenzoïques) par les humeurs et les organes d’Helix pomatia L. Thérapie 8, 744–748 (1953).

    CAS  PubMed  Google Scholar 

  • Bayliss, B. J., and A. Todrick: The use of a selective acetylcholinesterase inhibitor in the estimation of pseudocholinesterase activity in rat brain. Biochem. J. 62, 62–67 (1956).

    CAS  PubMed  Google Scholar 

  • Beckett, E. B., and G. H. Bourne: Histochemical demonstration of cholinesterase and 5-nucleotidase in normal and diseased human muscle. Nature (Lond.) 179, 771–772 (1957).

    Article  CAS  Google Scholar 

  • Belli, R., and S. Zazo: Micromethod for the determination of serum cholinesterase (Italian). Rif. med. 69, 1076–1080 (1955).

    CAS  Google Scholar 

  • Bergmann, F.: Fine structure of the active surface of cholinesterases and the mechanism of enzymatic ester hydrolysis. Disc. Faraday. Soc. 20, 126–134 (1955).

    Article  Google Scholar 

  • Bergmann, F.: The structure of the active surface of cholinesterases and the mechanism of their catalytic action in ester hydrolysis. Advanc. Catalysis 10, 130–164 (1958).

    Article  CAS  Google Scholar 

  • Bergmann, F. S. Rimon and R. Segal: Effect of pH on the activity of eel esterase towards different substrates. Biochem. J. 68, 493–499 (1958).

    CAS  PubMed  Google Scholar 

  • Bergmann, F. and R. Segal: The characterization of tissue cholinesterases. Biochim. biophys. Acta 16, 513–519 (1955).

    CAS  Google Scholar 

  • Bergmann, F. and R. Segal and S. Rimon: A new type of esterase in hog-kidney extract. Biochem. J. 67, 481–486 (1957).

    CAS  PubMed  Google Scholar 

  • Bergmann, F. and R. Segal A. Shimoni and M. Wurzel: The pH-dependence of enzymic ester hydrolysis. Biochem. J. 63, 684–690 (1956).

    CAS  PubMed  Google Scholar 

  • Bergmann, F. and R. Segal and M. Wurzel: The structure of the active surface of serum cholinesterase. Biochim. biophys. Acta 13, 251–259 (1954).

    CAS  Google Scholar 

  • Bernhard, S. A.: A simple model of molecular specificity in enzyme-substrate systems. I. Theory and applications to the system acetylcholinesterase-substrate. II. The correlation of the Michaelis constant with the inhibition constant. J. Amer. chem. Soc. 77, 1966–1972, 1973–1974 (1955).

    Google Scholar 

  • Bernsohn, J., and L. Possley: Butyrylcholinesterase in human and ruminant nervous tissue. Neurology 8, Suppl. 1, 94–95 (1958).

    Google Scholar 

  • Berry, J. F., and V. P. Whittaker: The acyl-group specificity of choline acetylase. Biochem. J. 73, 447–458 (1959).

    CAS  PubMed  Google Scholar 

  • Biggs, H. G., S. Carey and D. B. Morrison: A simple colorimetric method for measuring activities of cellular and plasma cholinesterase. Amer. J. clin. Path. 30, 181–186 (1958); Techn. Bull. Registry med. Techn. 28, 137–142 (1958).

    CAS  Google Scholar 

  • Blaschko, H., E. Bülbring and T. C. Chou: Tubocurarine antagonism and inhibition of cholinesterases. Brit. J. Pharmacol. 4, 29–32 (1949).

    CAS  PubMed  Google Scholar 

  • Blaschko, H., E. T. C. Chou and I. Wajda: The affinity of atropine-like esters for esterases. Brit. J. Pharmacol. 2, 108–115 (1947).

    CAS  PubMed  Google Scholar 

  • Bleisch, V. R., and H. Shwachman: Serum cholinesterase values in childhood in health and disease. Pediatrics 13, 426–438 (1954).

    CAS  PubMed  Google Scholar 

  • Blumenthal, H., and G. Woodard: Comparison of plasma triglyceride esterases and cholinesterases in various species. Fed. Proc. 16, 283 (1957).

    Google Scholar 

  • Bodansky, O.: Cholinesterase. Ann. N. Y. Acad. Sci. 47, 521–547 (1946).

    Article  CAS  Google Scholar 

  • Boell, E. J., and S.-C. Shen: Functional differentiation in embryonic development. I. Cholinesterase activity of induced neural structures in Amblystoma punctatum. J. exp. Zool. 97, 21–41 (1944).

    CAS  Google Scholar 

  • Bonting, S. L., and R. M. Featherstone: Ultramicro assay of the cholinesterases. Arch. Biochem. 61, 89–98 (1956).

    Article  CAS  PubMed  Google Scholar 

  • Bovet-Nttti, F.: Sur la nature de l’estérase contenue dans le venin de cobra. Experientia (Basel) 3, 283 (1947).

    Article  Google Scholar 

  • Broca, J.: Le dosage de la cholinestérase comme test de diagnose du sérum de cheval et de son état de conservation. Montauban.Imprimerie Forestié 1948.

    Google Scholar 

  • Brown, H. V., and A. F. Busc: Parathion inhibition of cholinesterase. Arch. indust. Hyg. 1, 633–636 (1950).

    CAS  Google Scholar 

  • Buckles, J., and K. Bullock: The application of enzyme inhibition to the estimation of small quantities of drugs possessing anticholinesterase activity. The assay of injection of neostigmine methylsulphate. J. Pharm. (Lond.) 8, 946–955 (1956).

    Article  CAS  Google Scholar 

  • Bullock, K.: The anticholinesterase activity of certain cytotoxic substances. Chem. Indust. 1955, 36–38.

    Google Scholar 

  • Burgen, A. S. V., and F. Hobbiger: The inhibition of cholinesterases by alkylphosphates and alkylphenolphosphates. Brit. J. Pharmacol. 6, 593–605 (1951).

    CAS  PubMed  Google Scholar 

  • Caraway, W. T.: Photometric determination of serum cholinesterase activity. Amer. J. clin. Path. 26, 945–955 (1956).

    CAS  Google Scholar 

  • Casida, J. E.: Comparative enzymology of certain insect acetylesterases in relation to poisoning by organophosphorus insecticides. Biochem. J. 60, 487–496 (1955).

    CAS  PubMed  Google Scholar 

  • Casier, H., et G. R. DE Vleeschhouwer: Sur les propriétés anti-cholinestérasiques et pharmacologiques du bromure de N-p-chloro-phenyl-méthyl-carbamate de m-hydroxyphényl-triméthylammonium (Nu-1250). Arch. int. Pharmacodyn. 90, 412–420 (1952).

    CAS  Google Scholar 

  • Cervini, C.: Simple alcalimetric method for the determination of serum cholinesterase activity (Italian). Minerva med. (Torino) 41, I, 456–458 (1950).

    Google Scholar 

  • Chadwick, L. E., and D. L. Hill: Inhibition of cholinesterase by di-isopropyl fluorophosphate, physostigmine and hexaethyl tetraphosphate in the roach. J. Neurophysiol. 10, 235–246 (1947).

    CAS  Google Scholar 

  • Chaudhuri, D. K.: Studies on cholinesterase. Ann. Biochem. exp. Med. 4, 77–86 (1944); 6, 91–94 (1946).

    CAS  Google Scholar 

  • Chessick, R. D.: The histochemical specificity of cholinesterases. J. Histochem. Cytochem. 2, 258–273 (1954).

    Article  CAS  PubMed  Google Scholar 

  • Chouteau, J., P. Rancien et A. Karamanian: Recherches sur les estérases du sérum sanguin. I. Méthode de détermination des activités cholinestérasique et tributyrinasique sérique. Bull. Soc. Chim. biol. (Paris) 38, 1329–1336 (1956).

    CAS  Google Scholar 

  • Cohen, J. A., F. Kalsbeek and M. G. P. J. Warringa: Reversibility of the inhibition of true cholinesterase by physostigmine. Biochim. biophys. Acta 2, 549–560 (1948).

    CAS  Google Scholar 

  • Cohen, J. A. and M. G. P. J. Warringa: Purification of cholinesterase from ox red cells. Biochim. biophys. Acta 10, 195–196 (1953).

    CAS  Google Scholar 

  • Cohen, J. A. and M. G. P. J. Warringa: The labelling of human serum by 32P-diisopropylphosphorofluoridate (DF32P). Biochim. biophys. Acta 25, 600–607 (1957).

    CAS  Google Scholar 

  • Cook, J. W.: Report on determination of insecticides by enzymatic methods. J. Ass. agric. Chem. (Wash.) 37, 561–564 (1954).

    CAS  Google Scholar 

  • Cook, J. W.: Paper chromatography of some organic phosphate insecticides. IV. Spot test for in vitro cholinesterase inhibitors. J. Ass. agric. Chem. (Wash.) 38, 150–153 (1955).

    CAS  Google Scholar 

  • Courville, D. A., and W. Ledington: A new method of assay for serum esterase. J. biol. Chem. 190, 575–584 (1951).

    CAS  PubMed  Google Scholar 

  • Croxatto, H., R. Croxatto and F. Huinobro: New photometric method for determination of cholinesterase activity of serum (Portuguese). An. Acad. Biol. Univ. Chile 3, 55–65 (1939).

    CAS  Google Scholar 

  • Dale, H. H.: The action of certain esters and ethers of choline and their relation to muscarine. J. Pharmacol. exp. Ther. 6, 147–190 (1914).

    CAS  Google Scholar 

  • Davies, D. R.: Cholinesterases and the mode of action of some anticholinesterases. J. Pharm. (Lond.) 6, 1–26 (1954).

    Article  Google Scholar 

  • Davies, D. R. and A. L. Green: The mechanism of hydrolysis by cholinesterase and related enzymes. Advanc. Enzymol. 20, 283–318 (1958).

    CAS  Google Scholar 

  • Davies, D. R. and J. D. Nicholls: A field test for the assay of human whole-blood cholinesterase. Brit. med. J. 1955 I, 1373–1375.

    Article  Google Scholar 

  • Davies, D. R. J. E. Risley and J. P. Rutland: The hydrolysis of choline esters by tissues of the ruminant. Biochem. J. 53, P 15 (1953).

    Google Scholar 

  • Davies, D. R. and J. P. RUTLAND: The electrometric method of Michel for the estimation of cholinesterases. Biochem. J. 47, P 22—P 23 (1950).

    Google Scholar 

  • Davison, A. N.: The reactions of rabbits to poisoning by p-nitrophenyldiethylphosphate (E 600). Brit. J. Pharmacol. 8, 208–211 (1953).

    Google Scholar 

  • Delaunois, A. L., et H. Casier: Micro-méthode potentiométrique pour la détermination de l’activité des cholinestérases. Arch. int. Pharmacodyn. 75, 371–381 (1948).

    CAS  Google Scholar 

  • Delcourt, A., et R. Hoeden: Pseudocholinestérase et affections hépatiques à propos d’une nouvelle technique de détermination. Acta gastro-ent. belg. 17, 102–109 (1954).

    CAS  Google Scholar 

  • Depierre, F., et A. Funke: Anticholinestérasiques. II. Dérivés analogues à la prostigmine. Influence de la structure chimique sur l’intensité et la sélectivité de l’action antiacétylcholinestérasique. C. R. Acad. Sci. (Paris) 239, 370–372 (1954).

    CAS  Google Scholar 

  • Diggle, W. M., and J. C. Gage: Cholinesterase inhibition in vitro by 0,0-diethyl 0-p-nitrophenyl thiophosphate (Parathion, E 605). Biochem. J. 49, 491–494 (1951).

    CAS  PubMed  Google Scholar 

  • Dyeing, O., and A. Hjelle: Cholinesterase activity in blood of cattle (Norwegian). Nord. Vet.-Med. 9, 41–48 (1957).

    Google Scholar 

  • Earl, C. J., and R. H. S. Thompson: Cholinesterase levels in the nervous system in triortho-cresyl phosphate poisoning. Brit. J. Pharmacol. 7, 685–694 (1952).

    CAS  PubMed  Google Scholar 

  • Einsel, D. W. jr., H. J. Trurorrr, S. D. Silver and E. C. Steiner: Self-equilibrating electro-lytic method for determination of acid production rates. Anal. Chem. 28, 408–410 (1956).

    Article  CAS  Google Scholar 

  • Eley, D. D., and G. S. Stone: Kinetic investigations on pseudo-cholinesterase. Biochem. J. 49, P 30 (1951).

    Google Scholar 

  • Ellis, S.: Benzoylcholine and atrophie esterase. J. Pharmacol. exp. Ther. 91, 370–378 (1947).

    CAS  PubMed  Google Scholar 

  • Ellis, S. Enzymic hydrolysis of morphine esters. J. Pharmacol. exp. Ther. 94, 130–135 (1948).

    Google Scholar 

  • Ferrari, W.: Insensitivity of chicken cholinesterase to specific inhibitors of true-and pseudo-enzyme. Nature (Lond.) 180, 144 (1957).

    Article  Google Scholar 

  • Fleisher, J H, and E. J. Pope: Colorimetric method for determination of red blood cell cholinesterase activity in whole blood. Arch. indust. Hyg. 9, 323–334 (1954).

    CAS  Google Scholar 

  • Fleisher, J H, and E. J. Pope and S. F. SPEAR: Determination of red blood cell cholinesterase activity in whole blood. An application of the colorimetric method to the blood of the rabbit, rat, pig, dog, goat, and monkey. Arch. indust. 111th 11, 332–337 (1955).

    Google Scholar 

  • Fleisher, J H S. Spear and E. J. Pope: Stable cholinesterase preparations as laboratory standards of activity. Anal. Chem. 27, 1080–1083 (1955).

    Article  Google Scholar 

  • Fleisher, J H G. S. Woodson and L. Simet: A visual method for estimating blood cholinesterase activity. Arch. indust. Hlth 14, 510–520 (1956).

    Google Scholar 

  • Frawley, J. P., and H. N. Fuyat: Effect of low dietary levels of parathion and systox on blood cholinesterase of dogs. J. Agric. Food Chem. 5, 346–348 (1957).

    Article  CAS  Google Scholar 

  • Frawley, J. P., and H. N. Fuyat E. C. Hagan and O. G. Fitzhugh: A comparative pharmacological and toxicological study of organic phosphate-anticholinesterase compounds. J. Pharmacol. exp. Ther. 105, 156 to 165 (1952).

    Google Scholar 

  • Fredriksson, T., and G. Tibblrng: Inhibition of cholinesterase with methylfluorophosphorylcholine and -carbocholine. Spontaneous return of activity. Biochem. Pharmacol. 3, 184 to 189 (1960).

    Google Scholar 

  • Friend, D. G., and O. Krayer: The estimation by a manometric method of the activity of cholinesterase in lymph. J. Pharmacol. exp. Ther. 71, 246–252 (1941).

    CAS  Google Scholar 

  • Fryer, J. H., R. G. D. Steel and H. H. Wiliiams: Cholinesterase activity levels in normal human subjects. A statistical evaluation with reference to the detection of minimal absorption of the organic phosphate insecticides. Arch. indust. Hlth 12, 406–411 (1955).

    CAS  Google Scholar 

  • Fulton, M. P., and G. A. Mogey: Some selective inhibitors of true cholinesterase. Brit. J. Pharmacol. 9, 138–144 (1954).

    CAS  PubMed  Google Scholar 

  • Funke, A., J. Bagot et F. Depierre: Anticholinestérasiques. I. Synthèse de diphénoxyalcanes porteurs d’une ou deux fonctions phénoliques libres. C. R. Acad. Sci. (Paris) 239, 329–331 (1954).

    CAS  Google Scholar 

  • Funke, A. J. Jacob et K. vox Däniken: Propriétés analgésiques et anticholinestérasiques du dichlorhydrate et du diiodométhylate de la bis-(pipéridinométhyl-coumaranyl-5) cétone. C. R. Acad. Sci. (Paris) 236, 149–151 (1953).

    CAS  Google Scholar 

  • Gal, E. M., and E. Roth: Spectrophotometric methods for determination of cholinesterase activity. Clin. chim. Acta 2, 316–326 (1957).

    CAS  Google Scholar 

  • Gal, I.: Choline-esterase and vegetative nervous system; new method for determination of choline-esterase activity of blood. Budap. Orv. Ujsag 37, 391–394 (1939).

    Google Scholar 

  • Gal, I.: Une nouvelle technique de dosage de l’activité cholinestérasique du sérum sanguin. Ann. Biol. clin. 6, 363–365 (1948).

    CAS  Google Scholar 

  • Gal, I. and L. VEGH: Etude de l’activité cholinestérasique du sérum sanguin par la méthode néphélometrique. Ann. Biol. clin. 6, 366–367 (1948).

    CAS  Google Scholar 

  • Ghosh, B. N., and N. K. Sarkar: Active principles of snake venoms. Amer. Ass. Advanc. Sci. 44, 189–196 (1956).

    Google Scholar 

  • Giacobini, E.: The distribution and localization of cholinesterases in nerve cells. Acta physiol. scand. 45, Suppl. 156, 1–45 (1959).

    Google Scholar 

  • Giang, P. A., and S. A. Hall: Enzymatic determination of organic phosphorus insecticides. Anal. Chem. 23, 1830–1834 (1951).

    Article  CAS  Google Scholar 

  • Glick, D.: Properties of choline esterase in human serum. Biochem. J. 31, 521–525 (1937).

    CAS  PubMed  Google Scholar 

  • Glick, D.: Studies on enzymatic histochemistry. XXV. A micro method for the determination of choline esterase and the activity-pH relationship of this enzyme. J. gen. Physiol. 21, 289–295 (1938 a).

    Google Scholar 

  • Glick, D.: Studies on the specificity of choline esterase. J. biol. Chem. 125, 729–739 (1938b).

    CAS  Google Scholar 

  • Glick, D.: Further studies on the specificity of choline esterase. J. biol. Chem. 130, 527–534 (1939).

    CAS  Google Scholar 

  • Glick, D.: Some additional observations on the specificity of choline esterase. J. biol. Chem. 137, 357–362 (1941).

    CAS  Google Scholar 

  • Glick, D.: The controversy on cholinesterase. Science 102, 100 (1945).

    Article  CAS  PubMed  Google Scholar 

  • Glick, D., S. Glaubach and D. H. Moore: Azolesterase activities of electrophoretically separated proteins of serum. J. biol. Chem. 144, 525–528 (1942).

    CAS  Google Scholar 

  • Goldstein, A.: The mechanism of enzyme-inhibitor-substrate reactions. Illustrated by the cholinesterase-physostigmine-acetylcholine system. J. gen. Physiol. 27, 529–580 (1944).

    Article  CAS  PubMed  Google Scholar 

  • Goldstein, A.: A “free manometer” technique for use with the Warburg apparatus. Proc. A.er. Acad. Arts Sci. 77, 235–253 (1949).

    Google Scholar 

  • Goldstein, A.: Cholinesterase specificity patterns in the tissues of man, cat, and teleost fish. J. Pharmacol. exp. Ther. 101, 13 (1951).

    Google Scholar 

  • GOLZ, H. H.: Anticholinesterase activity. Recognition and detection in the field and hospital. Arch. indust. Hlth 18, 138–141 (1958).

    CAS  Google Scholar 

  • Gomori, G.: The histochemistry of esterases. Int. Rev. Cytol. 1, 323–335 (1952).

    Article  Google Scholar 

  • Goldstein, A.: Histochemistry of human esterases. J. Histochem. Cytochem. 3, 479–484 (1955).

    Article  Google Scholar 

  • Gordon, J. J.: N-Diethylaminoethylphenothiazine a specific inhibitor of pseudocholinesterase. Nature (Lond.) 162, 146 (1948).

    Article  CAS  Google Scholar 

  • Goutier, R.: Etude électrophoretique des estérases sériques et de la fixation du DF32P dans le sérum, chez le lapin et le cobaye. Biochim. biophys. Acta 19, 524–534 (1956).

    CAS  Google Scholar 

  • Greenberg, S., and C. Calvert: Modification of Michel method for cholinesterase determina-tion. Med. Techn. Bull. 8, 59–64 (1957).

    CAS  PubMed  Google Scholar 

  • Grégoire, J., et M. Cotte: Test spectrophotométrique des cholinestérases sériques. C.R. Soc. Biol. (Paris) 146, 741–744 (1952).

    Google Scholar 

  • Grégoire, J., et M. Cotte J. Grégoire et N. Limozin: Sur l’activité des cholinestérases. I. Méthode de dosage spectrophotométrique de l’activité des cholinestérases. Bull. Soc. Chim. biol. (Paris) 37, 65–79 (1955 a).

    Google Scholar 

  • Grégoire, J., et M. Cotte J. Grégoire et N. Limozin: Sur l’activité des cholinestérases. II. Application de la méthode spectrophotométrique à l’étude cinétique de l’activité des cholinestérases purifiées aux très faibles concentrations en substrat. Bull. Soc. Chim. biol. (Paris) 37, 81–87 (1955b).

    Google Scholar 

  • Grégoire, J., et M. Cotte J. Grégoire et N. Limozin N. Limozin et J. Grégoire: Sur l’activité des cholinestérases. III. Application de la méthode spectrophotométrique à l’influence des concentrations salines sur l’affinité des cholinestérases purifiées vis-à-vis de l’acétylcholine. Bull. Soc. Chim. biol. (Paris) 38, 147–163 (1956).

    Google Scholar 

  • Greig, M. E., and A. J. Gibbons: Cation transport in erythrocytes treated with lecithinase A. Arch. Biochem. 61, 343–347 (1956).

    Article  CAS  PubMed  Google Scholar 

  • Gouter, J. M.: Absence of pseudo-cholinesterase from the tissues of ruminants Nature (Lond.) 157, 369 (1946).

    Google Scholar 

  • Hagan, E. C., P. M. Jenner, W. I. Jones and O. G. Fitzhugh: Blood withdrawal and processing preparatory to plasma and cell cholinesterase determinations in rats. J. Ass. agric. Chem. (Wash.) 41, 899 (1958).

    CAS  Google Scholar 

  • Hall, G. E., and C. C. Lucas: Choline esterase activity of normal and pathological human sera. J. Pharmacol. exp. Ther. 59, 34–42 (1937).

    CAS  Google Scholar 

  • Hamblin, D. O., and J. F. Marchand: Cholinesterase tests and their applicability in the field. Amer. Cyanamid Co., New York, March 1951.

    Google Scholar 

  • Hardegg, W., D. Bechinger U. R. Dohrmann: Zur Bedeutung der Gleichung von Schaefer für unsere Auffassung über die Kinetik bei Cholinesterases. Pflügers Arch. ges. Physiol. 263, 33–47 (1956).

    CAS  Google Scholar 

  • Hardegg, W. u. R. Poche: Bemerkungen zur Kinetik und Substratspezifität der Cholinesterasen (Vorläufige Mitteilung). Klin. Wschr. 30, 799–800 (1952).

    Article  CAS  PubMed  Google Scholar 

  • Hardegg, W. u. H. Schaefer: Zur Kinetik der Cholinesterases. Mit einer Verbesserung der Warburgschen Apparatur. Pflügers Arch. ges. Physiol. 255, 136–153 (1952).

    CAS  Google Scholar 

  • Harpers, C. L., and J. M. Van Mulken: Simple determination of pseudocholinesterase activity in blood serum (Dutch). Pharm. Weekblad 89, 845–848 (1954).

    Google Scholar 

  • Hardwick, D. C.: Cholinesterases in bovine plasma. Biochem. J. 64, P 1 (1956).

    Google Scholar 

  • Hargreaves, A. B.: Action of acetate ion on hydrolysis of acetylcholine and its application to the titrimetric determination of cholinesterase (Spanish). An. Acad. bras. tient. 25, 291–301 (1953).

    CAS  Google Scholar 

  • Hargreaves, A. B. C. Calmon Lemme and L. Ludmila Liepin: Experiments on the acetylcholinesterase of the electric organ of the Electrophorus electricus. An. Acad. bras. tient. 31, 59–66 (1959).

    Google Scholar 

  • Hargreaves, A. B. and L. C. G. Lobo: An improved step in the method of Rothenberg and Nachmansohn for the purification of acetylcholinesterase from electric tissue. Arch. Biochem. 46, 481–482 (1953).

    Google Scholar 

  • Hargreaves, A. B. and L. C. G. Lobo: Titrimetric determination of cholinesterase in blood serum (Spanish). Hospital (Rio de J.) 55, 99–106 (1959).

    CAS  Google Scholar 

  • Harris, H., and M. Whittaker: Differential response of human serum cholinesterase types to an inhibitor in potato. Nature (Lond.) 183, 1808 (1959).

    Article  CAS  Google Scholar 

  • Hawkins, R. D., and J. M. Gunter: Studies on cholinesterase. 5. The selective inhibition of pseudo-cholinesterase in vivo. Biochem. J. 40, 192–197 (1946).

    CAS  Google Scholar 

  • Hawkins, R. D., and B. Mendel: True cholinesterases with pronounced resistance to eserine. J. Cell. comp. Physiol. 27, 69–85 (1946).

    Article  CAS  Google Scholar 

  • Hawkins, R. D., and B. Mendel: Selective inhibition of pseudo-cholinesterase by diisopropyl fluorophosphonate. Brit. J. Pharmacol. 2, 173–180 (1947).

    CAS  PubMed  Google Scholar 

  • Hawkins, R. D., and B. Mendel: Studies on cholinesterase. 6. The selective inhibition of true cholinesterase in vivo. Biochem. J. 44, 260–264 (1949).

    CAS  Google Scholar 

  • Heilbronn, E.: Hydrolysis of carboxylic acid esters of thiocholine and its analogues. 1 and 2. Acta chem. scand. 12, 1481–1491, 1492–1506 (1958).

    Google Scholar 

  • Heilbronn, E.: Hydrolysis of carboxylic acid esters of thiocholine and its analogues. 3. Hydrolysis catalysed by acetylcholine esterase and butyrylcholine esterase. Acta chem. scand. 13, 1547–1560 (1959).

    Article  CAS  Google Scholar 

  • Herzfeld, E., u. C. Stumpf: Ein neuer Kurztest zur Bestimmung der Serumcholinesteraseaktivität. Wien. klin Wschr. 67, 874–876 (1955).

    CAS  PubMed  Google Scholar 

  • Hestrin, S.: The reaction of acetylcholine and carboxylic acid derivatives with hydroxyl-amine, and its analytical application. J. biol. Chem. 180, 249–261 (1949).

    CAS  PubMed  Google Scholar 

  • Hines, B. E., and R. A. Mccance: Pseudo-cholinesterase activity in secretions and organsof piglets and pigs. J. Physiol. (Lond.) 122, 188–192 (1953).

    Google Scholar 

  • Hobbigger, E. E.: The hydrolysis of indoxyl esters by rat esterases. Biochem. J. 67, 600–607 (1957).

    Google Scholar 

  • Hofstee, B. H. J.: Spectrophotometric determinations of esterases. Science 114, 128–130 (1951).

    Article  CAS  PubMed  Google Scholar 

  • Holmstedt, B.: Pharmacology of organophosphorus cholinesterase inhibitors. Pharmacol. Rev. 11, 567–688 (1959).

    CAS  PubMed  Google Scholar 

  • Holt, S. J.: The value of fundamental studies of staining reactions in enzyme histochemistry, with reference to indoxyl methods for esterases. J. Histochem. Cytochem. 4, 541–554 (1956).

    Article  CAS  PubMed  Google Scholar 

  • Holton, P.: The enzymic hydrolysis of triacetin. Biochem. J. 43, P 13 (1948).

    Google Scholar 

  • Homann, W Eine papierchromatographische Methode zur Messung der Cholinesterase-

    Google Scholar 

  • aktivität. Naunyn-Schmiedeberg’s Arch. exp. Path. Pharmak. 224, 176–178 (1955).

    Google Scholar 

  • Huc, M.: Recherches sur la détermination et la signification de l’activité procainestérasique du sérum humain. Lille Douriez-Bataille 1950.

    Google Scholar 

  • Huerga, J. De La, C. Yesinick and H. Popper: Colorimetrie method for the determination of serum cholinesterase. Amer. J. clin. Path. 22, 1126–1133 (1952).

    Google Scholar 

  • Inagaki, K., M. Morita, M. Iguchi and S. Tsuda: The extraction of erythrocyte cholin-esterase with chlorophyllin solution. Yokohama med. Bull. 4, 358–364 (1953).

    CAS  Google Scholar 

  • Jacob, J.: Sur l’inhibition sélective des acétylcholinestérases in vivo chez le chien. Experientia (Basel) 10, 33–34 (1954).

    Article  CAS  Google Scholar 

  • Jacob, J.: Propriétés antiacétylcholinestérasiques spécifiques du di-iodo-méthylate de la bis-(piperidinométhylcoumaranyl-5) cétone (3318 CT). I—II. Arch. int. Pharmacodyn. 101, 446–468 (1955); 106, 395–436 (1956).

    CAS  Google Scholar 

  • Jacobsohn, K. P., et J. Tapadinhas: Action des métaux lourds sur la cholinestérase. Bull. Soc. port. Sci. nat. 14, 103–106 (1943).

    Google Scholar 

  • Jensen-Holm, J., H. H. Lausen, K. Milthers and K. O. Moller: Determination of the cholinesterase activity in blood and organs by automatic titration. With some observations of serious errors of the method and remarks of the photometric determination. Acta pharmacol. (Kbh.) 15, 384–394 (1959).

    Article  CAS  Google Scholar 

  • Kalow, W.: Zur Kenntnis der Butryrylcholin-Esterase im Serum von Mensch und Pferd. Naunyn-Schmiedeberg’s Arch. exp. Path. Pharmak. 215, 370–377 (1952 a).

    Google Scholar 

  • Kalow, W.: Hydrolysis of local anesthetics by human serum cholinesterase. J. Pharmacol. exp. Ther. 104, 122–134 (1952).

    CAS  PubMed  Google Scholar 

  • Kalow, W. and R. O. Davies: The activity of various esterase inhibitors towards atypical human serum cholinesterase. Biochem. Pharmacol. 1, 183–192 (1958).

    Article  Google Scholar 

  • Kalow, W. and K. GENEST: A method for the detection of atypical forms of human serum cholinesterase. Determination of Dibucaine Numbers. Canad. J. Biochem. 35, 339–346 (1957).

    CAS  PubMed  Google Scholar 

  • Kalow, W. and N. Staron: Kinetic studies on the hydrolysis of benzolcholine by human serum cholinesterase. Canad. J. Biochem. 34, 637–653 (1956).

    Article  CAS  PubMed  Google Scholar 

  • Kalow, W. and D. R. Gunn: The relation between dose of succinylcholine and duration of apnea in man. J. Pharmacol. exp. Ther. 120, 203–214 (1957).

    CAS  PubMed  Google Scholar 

  • Kalow, W. and D. R. Gunn: Some statistical data on atypical cholinesterase of human serum. Ann. human. Genet. 23, 239–250 (1959).

    Article  CAS  Google Scholar 

  • Kalow, W. and D. R. Gunn and H. A. Lindsay: A comparison of optical and manometric methods for the assay of human serum cholinesterase. Canad. J. Biochem. 33, 568–574 (1955).

    Article  CAS  PubMed  Google Scholar 

  • Kalow, W. and D. R. Gunn and H. A. Lindsay: Abnormal behavior of human serum cholinesterase. J. Pharmacol. exp. Ther. 116, 34 (1956).

    Google Scholar 

  • Kalow, W. and D. R. Gunn and H. A. Lindsay and N. Staron: On distribution and inheritance of atypical forms of human serum cholinesterase, as indicated by dbucaine numbers. Canad. J. Biochem. 35, 1305–1320 (1957).

    Article  CAS  PubMed  Google Scholar 

  • Karczmar, A. G., T. Koppawyi and G. C. SHEATZ: Further studies on intravenously injected cholinesterase preparations. J. Pharmacol. exp. Ther. 107, 501–518 (1953).

    CAS  PubMed  Google Scholar 

  • Katsh, S.: Anticholinesterase activity of drugs assayed by a rapid colorimetric method. J. appl. Physiol. 8, 215–219 (1955).

    CAS  PubMed  Google Scholar 

  • Kaufman, K.: Serum cholinesterase activity in the normal individual and in people with liver disease. Ann. intern. Med. 41, 533–545 (1954).

    Article  CAS  PubMed  Google Scholar 

  • Kekwick, R. G. O., M. E. Mackay and N. H. MARTIN: The preliminary isolation and char-acterization of human serum cholinesterase. Biochem. J. 53, P 36—P 37 (1953).

    Google Scholar 

  • Koelle, G. B.: The histochemical differentiation of types of cholinesterases and their local-izations in tissues of the cat. J. Pharmacol. exp. Ther. 100, 158–179 (1950).

    CAS  PubMed  Google Scholar 

  • Koelle, G. B.: The elimination of enzymatic diffusion artifacts in the histochemical localization of cholinesterases and a survey of their cellular distributions. J. Pharmacol. exp. Ther. 103, 153 to 171 (1951).

    Google Scholar 

  • Koelle, G. B.: Cholinesterases of the tissues and sera of rabbits. Biochem. J. 53, 217–226 (1953).

    CAS  PubMed  Google Scholar 

  • Koelle, G. B.: The histochemical localization of cholinesterases in the central nervous system of the rat. J. comp. Neurol. 100, 211–235 (1954).

    Article  CAS  PubMed  Google Scholar 

  • Koelle, G. B.: Histochemical demonstration of reversible anticholinesterase action at selective cellular sites in vivo. J. Pharmacol. exp. Ther. 120, 488–503 (1957).

    CAS  PubMed  Google Scholar 

  • Koelle, G. B. and A. Gilman: Anticholinesterase drugs. J. Pharmacol. exp. Ther. 95 (Part II, Pharmacol. Rev.), 166–216 (1949).

    CAS  PubMed  Google Scholar 

  • Köver, A., and T. Kovacs: On the specificity of myosincholinesterase. Acta physiol. Acad. Sci. hung. 11, 259–265 (1957).

    Google Scholar 

  • Köver, A., and T. Kovacs and T. König: On the properties of myosincholinesterase. Acta physiol. Acad. Sci. hung. 11, 253–258 (1957).

    Google Scholar 

  • Kooistra, G.: Contribution to the knowledge of the action of acetylcholine in the intestine of Periplaneta americana L. Physiol. comp. oecol. 2, 75–80 (1949).

    Google Scholar 

  • Kramer, D. N., and R. M. Gamson: Colorimetric determination of acetylcholinesterase activity. Anal. Chem. 30, 251–254 (1958).

    Article  CAS  Google Scholar 

  • Kuroda, K., M. Fujino and K. Irino: A portable micromethod of the determination of cholinesterase activity in blood serum. Tokushima J. exp. Med. 6, 73–80 (1959).

    CAS  Google Scholar 

  • Lalli, G., and L. Cascino: Colorimetric method for the determination of cholinesterase activity in plasma and red blood cells (Italian). Riv. Med. aero. 19, 103–137 (1956).

    Google Scholar 

  • Lands, A. M., J. O. Hoppe, A. Arnold and F. K. Kirchner: An investigation of the structure-activity correlations within a series of ambenonium analogs. J. Pharmacol. 123, 121–127 (1958).

    CAS  Google Scholar 

  • Larsson, L., and B. Hansen: An automatic recording titrator. S vensk kem.T. 68, 521–527 (1956).

    CAS  Google Scholar 

  • Lawler, H. C.: A simplified procedure for the partial purification of acetylcholinesterase from electric tissue. J. biol. Chem. 234, 799–801 (1959).

    Google Scholar 

  • Lehmann, H., V. Patston and E. Ryan: The inheritance of an idiopathic low plasma pseudo-cholinesterase level. J. clin. Path. 11, 554 (1958).

    Google Scholar 

  • Lehmann, H., V. Patston and E. Ryan and E. Ryan: The familial incidence of low pseudocholinesterase level. Lancet 1956 II, 124.

    Article  Google Scholar 

  • Lehmann, H., V. Patston and E. Ryan and P. H. Simmons: Sensitivity to suxamethonium. Apnoe in two brothers. Lancet 1958 II, 981–982.

    Article  Google Scholar 

  • Lesuk, A.: Stabilized cholinesterase. U.S. Pat. 2,475,792-2,475,793, July 12, 1949.

    Google Scholar 

  • Levine, M. G., and A. A. Suran: A new cholinesterase in swine serum. Nature (Lond.) 166, 698 (1950).

    Article  CAS  Google Scholar 

  • Levine, M. G., and A. A. Suran: A survey of some mammalian serum cholinesterases. Enzymologia 15, 17–20 (1951).

    CAS  PubMed  Google Scholar 

  • Levy, J.: Sur les estérases du sérum humain. J. Physiol. (Paris) 43, 103–125 (1951 a).

    Google Scholar 

  • Levy, J.: Sur les estérases du sérum de lapin. J. Physiol. (Paris) 43, 127–138 (1951 b).

    Google Scholar 

  • Levy, J.: Sur les estérases du sang de rat. J. Physiol. (Paris) 43, 217–222 (1951 c).

    Google Scholar 

  • Levy, J.: Sur la benzoylcholinestérase. J. Physiol. (Paris) 43, 783–784 (1951d).

    CAS  Google Scholar 

  • Levy, J. et B. Tchoubar: Relations entre la vitesse d’hydrolyse de divers esters de la choline par la benzoylcholinestérase et la constitution chimique des substrats. J. Physiol. (Paris) 44, 95–97 (1952).

    CAS  Google Scholar 

  • Limperos, G., and K. E. Ranta: A rapid screening test for the determination of the approxi- mate cholinesterase activity of human blood. Science 117, 453–455 (1953).

    Article  CAS  PubMed  Google Scholar 

  • Linderstrem-Lang, K., and D. Glick: Micromethod for determination of choline esterase activity. C. R. Lab. Carlsberg, Sér. chim. 22, 300–306 (1938).

    Google Scholar 

  • Lord, K. A., and C. Potter: Differences in esterases from insect species toxicity of organo-phosphorus compounds and in vitro anti-esterase activity. J. Sci. Food Agric. 5, 490–498 (1954).

    Article  CAS  Google Scholar 

  • Lowry, O. H., N. R. Roberts, M.-L. Wu, W. S. Hixon and E. J. Crawford: The quantitative histochemistry of brain. II. Enzyme measurements. J. biol. Chem. 207, 19–37 (1954).

    CAS  PubMed  Google Scholar 

  • Luna Perez, J. L.: A new method for determination of serum cholinesterase (Spanish). Rev. clin. esp. 61, 245–247 (1956).

    CAS  PubMed  Google Scholar 

  • Lunorn, S. J.: Acetylcholinesterase in goldfish muscles. Studies on some substrates and inhibitors. Biochem. J. 72, 210–214 (1959).

    Google Scholar 

  • Macdonald, W. E., C. B. Pollard and A. H. Gropp: A rapid micromethod for electrometric determination of red cell cholinesterase activity in whole blood. Arch. indust. Hyg. 6, 271–275 (1952).

    Google Scholar 

  • Malmstrom, B. G., Ü. Levin and H. G. Boman: Chromatography of human serum cholinesterase. Acta chem. scand. 10, 1077–1082 (1956).

    Article  CAS  Google Scholar 

  • Marchand, J. F.: Microtest for cholinesterase. Interpretation after nerve gas or agricultural insecticide exposures. J. Amer. med. Ass. 149, 738–740 (1952).

    Article  CAS  Google Scholar 

  • Marples, E. A., R. H. S. Thomeson and G. R. Webster: The liberation of active enzymes from brain tissue by lysolecithin. J. Neurochem. 4, 62–70 (1959).

    Article  CAS  PubMed  Google Scholar 

  • Mcosker, D. E., and L. J. Daniel: A colorimetric micro method for the determination of cholinesterase. Arch. Biochem. 79, 1–7 (1959).

    Article  CAS  Google Scholar 

  • Mendel, B., and R. D. Hawkins: Estimation of the cholinesterases. Meth. med. Res. 3, 107–115 (1950).

    Google Scholar 

  • Mendel, B., and R. D. Hawkins and D. B. Mundell: Studies on cholinesterase. 2. A method for the purification of a pseudo-cholinesterase from dog pancreas. Biochem. J. 37, 64–66 (1943).

    CAS  PubMed  Google Scholar 

  • Mendel, B., and R. D. Hawkins and H. Rudney: Cholinesterase. III. Specific tests for true cholinesterase and pseudo-cholinesterase. Biochem. J. 37, 473–476 (1943).

    CAS  PubMed  Google Scholar 

  • Mendel, B., and R. D. Hawkins and D. K. Myers: Identification of pseudocholinesterase in the tissues of ruminants. Nature (Lond.) 176, 783 (1955).

    Article  CAS  Google Scholar 

  • Mendel, B., and R. D. Hawkins and H. Rtdney: Studies on cholinesterase. 1. Cholinesterase and pseudo-cholinesterase. Biochem. J. 37, 59–63 (1943a).

    CAS  PubMed  Google Scholar 

  • Mendel, B., and R. D. Hawkins On the type of cholinesterase present in brain tissue. Science 98, 201–202 (1943b).

    Article  CAS  PubMed  Google Scholar 

  • Mendel, B., and R. D. Hawkins: The cholinesterases in the light of recent findings. Science 100, 499–500 (1944).

    Article  CAS  PubMed  Google Scholar 

  • Menghi, P., E. Grasso and V. Quinte: Methods for the determination of cholinesterase activity. Minerva pediat. (Torino) 5, 1039–1043 (1953).

    CAS  Google Scholar 

  • Mentha, J., H. Sprinz and R. Barnard: Rapid extraction of human erythrocyte cholinesterase by alkali pseudoagglutination. J. biol. Chem. 167, 623 (1947).

    CAS  PubMed  Google Scholar 

  • Metcalf, R. L.: The colorimetric microestimation of human blood cholinesterases and its application to poisoning by organic phosphate insecticides. J. econ. Ent. 44, 883–890 (1951).

    CAS  Google Scholar 

  • R. L. Metcalf, and R. B. March: Studies of the mode of action of parathion and its derivatives and their toxicity to insects. J. econ. Ent. 42, 721–728 (1949).

    CAS  Google Scholar 

  • R. L. Metcalf, and R. B. March: Properties of acetylcholine esterases from the bee, the fly and the mouse and their relation to insecticide action. J. econ. Ent. 43, 670–677 (1950).

    CAS  Google Scholar 

  • R. L. Metcalf, and R. B. March and M. G. Maxon: Substrate preferences of insect cholinesterases. Ann ent. Soc. Amer. 48, 222–228 (1955).

    CAS  Google Scholar 

  • Meyer, A., u. W. Wilbrandt: Zur Bestimmung der Aktivität der Cholinesterasen im menschlichen Blute. Helv. physiol. pharmacol. Acta 12, 206–216 (1954).

    CAS  Google Scholar 

  • Michel, H. O.: An electrometric method for the determination of red blood cell and plasma cholinesterase activity. J. Lab. clin. Med. 34, 1564–1568 (1949).

    CAS  Google Scholar 

  • Molander, D. W., M. M. Friedman and J. S. Ladite: Serum cholinesterase in hepatic and neoplastic diseases a preliminary report. Ann. intern. Med. 41, 1139–1151 (1954).

    Article  CAS  PubMed  Google Scholar 

  • Mommaerts, W. F. H. M., P. A. Khahrallah and M. F. Dickens: Acetylcholinesterase in the conductive tissue of the heart. Circulat. Res. 1, 460–465 (1953).

    Article  CAS  PubMed  Google Scholar 

  • Morand, P., et H. Laborrr: La mesure de l’activité cholinestérasique du sérum. Mise au point d’une méthode applicable à la clinique. Presse méd. 55, 131–132, 251 (1947).

    Google Scholar 

  • Morton, R. K.: Methods of extraction of enzymes from animal tissues. In; S. P. CoLowicK and N. O. KAPLAN, Eds., Methods in Enzymology, vol. I, 25–51. New York. Academic Press 1955.

    Google Scholar 

  • L. A. Mounter: The specificity of cobra-venom cholinesterase. Biochem. J. 50, 122–128 (1951).

    CAS  PubMed  Google Scholar 

  • L. A. Mounter: The complex nature of dialkylfluorophosphatases of hog and rat liver and kidney. J. biol. Chem. 215, 705–711 (1955).

    Google Scholar 

  • L. A. Mounter and V. P. Whittaker: The esterases of horse blood 2. The specificity of horse erythrocyte cholinesterase. Biochem. J. 47, 525–530 (1950).

    CAS  PubMed  Google Scholar 

  • L. A. Mounter and V. P. Whittaker: The hydrolysis of esters of phenol by cholinesterases and other esterases. Biochem. J. 54, 551–559 (1953).

    CAS  PubMed  Google Scholar 

  • Myers, D. K.: Effect of salt on the hydrolysis of acetylcholine by cholinesterases. Arch. Biochem. 37, 469–487 (1952).

    Article  CAS  PubMed  Google Scholar 

  • Myers, D. K.: Studies on cholinesterase. 9. Species variation in the specificity pattern of the pseudo cholinesterase. Biochem. J. 55, 67–79 (1953).

    CAS  PubMed  Google Scholar 

  • Myers, D. K.: Studies on Selective Esterase Inhibitors. ‘s-Gravenhage: Uitgeverij Excelsior 1954.

    Google Scholar 

  • Nacimansohn, D.: Die Rolle des Acetylcholins in den Elementarvorgängen der Nervenleitung. Ergebn. Physiol. 48, 575–683 (1955).

    Article  Google Scholar 

  • Myers, D. K.: Chemical and Molecular Basis of Nerve Activity. New York. Academic Press 1959.

    Google Scholar 

  • Myers, D. K. and M. A. Rothenberg: On the specificity of choline esterase in nervous tissue. Science 100, 454 (1944).

    Article  Google Scholar 

  • Myers, D. K. and M. A. Rothenberg: Studies on cholinesterase. I. On the specificity of the enzyme in nerve tissue. J. biol. Chem. 158, 653–666 (1945).

    Google Scholar 

  • Myers, D. K. and M. A. Rothenberg and H. Schneemann: On the effect of drugs on cholinesterase. J. biol. Chem. 159, 239 to 240 (1945).

    Google Scholar 

  • D. K. Myers, and M. A. Rothenberg and H. Schneemann and I. B. Wuson: The enzymic hydrolysis and synthesis of acethylcholine. Advanc. Enzymol. 12, 259–339 (1951).

    Google Scholar 

  • D. K. Myers, and M. A. Rothenberg and H. Schneemann and I. B. Wuson: Acetylcholinesterase. In; S. P. CoLOwrcx and N. O. KAPLAN, Eds., Methods in Enzymology, vol. I, 642–651. New York. Academic Press 1955.

    Google Scholar 

  • Neilands, J. B., and M. D. Cannon: Automatic recording pu instrumentation. Anal. Chem. 27, 29–33 (1955).

    Article  CAS  Google Scholar 

  • Ord, M. G., and R. H. S. Thompson: The distribution of cholinesterase types in mammalian tissues. Biochem. J. 46, 346–352 (1950).

    CAS  PubMed  Google Scholar 

  • Ord, M. G., and R. H. S. Thompson: The preparation of soluble cholinesterases from mammalian heart and brain. Biochem. J. 49, 191–199 (1951).

    CAS  PubMed  Google Scholar 

  • Ord, M. G., and R. H. S. Thompson: Pseudo-cholinesterase activity in the central nervous system. Biochem. J. 51, 245–251 (1952).

    CAS  PubMed  Google Scholar 

  • Orgell, W. H., K. A. Vaidya and P. A. Dahm: Inhibition of human plasma cholinesterase in vitro by extracts of Solanaceous plants. Science 128, 1136 (1958).

    Article  CAS  PubMed  Google Scholar 

  • Ormerod, W. E.: Hydrolysis of benzoylcholine derivatives by cholinesterase in serum. Biochem. J. 54, 701–704 (1953).

    CAS  PubMed  Google Scholar 

  • Paget, M., et G. Diellemmes: Sur le dosage de la pseudocholinestérase du sérum humain. Technique personelle. Ann Biol. clin. 5, 380–385 (1947).

    CAS  Google Scholar 

  • Pasqualin, R., and R. Moscovici: Colorimetric determination of cholinesterase in blood serum (Portuguese). Arch. Biol. (S. Paulo) 37, 59–65 (1953).

    CAS  Google Scholar 

  • Paulesu, F.: Differences in cholinesterase activity of various biological material. III. A new type of cholinesterase resistant to CT 3318 and eucupine (Italian). Arch. int. Pharmacodyn. 105, 366–380 (1956).

    CAS  Google Scholar 

  • Paulesu, F. L. VARGru e G. Gibertoni: Differences in cholinesterase activity of various biological material II Inhibitory effect of CT 3318 (Italian). Arch. in Pharmacodyn. 104, 11–18 (1955).

    Google Scholar 

  • Pighini, G.: Cholinesterase in various parts of the nervous system (Italian). Biochim. Terap. sper. 26, 157–159 (1939);

    CAS  Google Scholar 

  • Paulesu, F.: Boll. Soc. ital. Biol. sper. 15, 237–238 (1940).

    Google Scholar 

  • Pilz, W.: Untersuchungen über Fermente des menschlichen Blutes. I. Die photometrische Mikrobestimmung der Acetylcholinesterase in Serum und Erythrocyten. Klin. Wschr. 36, 1017–1021 (1958).

    Article  CAS  PubMed  Google Scholar 

  • Pinter, I.: Esterase activity of serum protein fractions. Acta physiol. Acad. Sci. hung. 11, 39–44 (1957).

    CAS  Google Scholar 

  • Plattner, F., u. H. Hintner: Die Spaltung von Acetylcholin durch Organextrakte und Körperflüssigkeiten. Pflügers Arch. ges. Physiol. 225, 19–25 (1930).

    Article  CAS  Google Scholar 

  • Pochet, A.: Mesures de l’activité cholinestérasique. J. Pharm. Belg. 10, 339–357 (1955).

    CAS  PubMed  Google Scholar 

  • Polonovski, M., I. Izzat and M. Robert: Méthode turbidimétrique pour le dosage de l’activité des estérases. Bull. Soc. Chim. biol. (Paris) 35, 225–230 (1953).

    CAS  Google Scholar 

  • Pribilla, O.: Die Bestimmung der Serumcholinesterase an der Leiche. Dtsch. Z. ges. gerichtl. Med. 46, 79–92 (1957).

    CAS  Google Scholar 

  • Radouco, C., et E. Frommel: Microméthode électrométrique pour la mesure de l’activité des cholinestérases. Helv. physiol. pharmacol. Acta 10, C 39 (1952).

    Google Scholar 

  • Rappaport, F., J. Fischl and N. Pinto: An improved method for the estimation of cholinesterase activity in serum. Clin. chin. Acta 4, 227–230 (1959).

    CAS  Google Scholar 

  • Ravin, H. A., K.-C. Tsou and A. M. Seligman: Colorimetric estimation and histochemical demonstration of serum cholinesterase. J. biol. Chem. 191, 843–857 (1951).

    CAS  PubMed  Google Scholar 

  • Ravin, H. A., K.-C. Tsou and A. M. Seligman S. I. ZACKS and A. M. S.ligman: The histochemical localization of acetylcholinesterase in nervous tissue. J. Pharmacol. exp. Ther. 107, 37–53 (1953).

    CAS  Google Scholar 

  • Reinhold, J. G., L. G. Tourigny and V. L. Yonan: Measurement of serum cholinesterase activity by a photometric indicator method. Together with a study of the influence of sex and race. Amer. J. clin. Path. 23, 645–653 (1953).

    CAS  Google Scholar 

  • Richards, A. G., and L. Cutkomp: Cholinesterase of insect nerves. J. cell. comp. Physiol. 26, 57–61 (1945).

    Article  CAS  Google Scholar 

  • Richter, D., and P. G. Croft: Blood esterases. Biochem. J. 36, 746–757 (1942).

    CAS  PubMed  Google Scholar 

  • Roan, C. C., and S. Maeda: The cholinesterase of the oriental fruit fly and its in vitro reactions with various insecticidal compounds. J. econ. Ent. 46, 775–779 (1953).

    CAS  Google Scholar 

  • Roan, C. C., and S. Maeda: The cholinesterase systems of three species of fruit flies and the effects of certain insecticidal compounds on these enzymes. J. econ. Ent. 47, 507 to 514 (1954).

    Google Scholar 

  • Rosnati, V., and F. Bovet-Nitti: Pharmacological properties and sensibility of esterases to various derivatives of benzoylcholine and phenylacetylcholine (Italian). R. C. Ist. sup. Sanità 18, 971–982 (1955).

    CAS  Google Scholar 

  • Rothenberg, M. A., and D. Nachmansohn: Studies on cholinesterase. III. Purification of the enzyme from electric tissue by fractional ammonium sulfate precipitation. J. biol. Chem. 168, 223–231 (1947).

    CAS  PubMed  Google Scholar 

  • Rubin, A. A., J. Mershon, M. E. Grelis and I. I. A. Tabachnick: A spectrophotometric method for assaying anticholinesterase activity. Fed. Proc. 16, 333 (1957).

    Google Scholar 

  • Sabine, J. C.: The clinical significance of erythrocyte cholinesterase titers. I. A method suitable for routine clinical use, and the distribution of normal values. Blood 10, 1132–1138 (1955).

    CAS  PubMed  Google Scholar 

  • Sack, A., and E. A. Zeller: New method of determination of the choline-esterase activity. Science 97, 449 (1943).

    Article  CAS  PubMed  Google Scholar 

  • Sailer, S., u. H. Braunsteiner: Über eine neue, sehr einfache Methode zur Bestimmung der Serumcholinesteraseaktivität und ihre klinische Bedeutung. Klin. Wschr. 37, 986–990 (1959).

    Article  CAS  PubMed  Google Scholar 

  • Sanz, M. C.: Bestimmung der Cholinesterase-Aktivität mit Glaselektrode. Helv. physiol. pharmacol. Acta 2, C 29—C 32 (1944).

    Google Scholar 

  • Sawyer, C. H.: Hydrolysis of choline esters by liver. Science 101, 385 (1945).

    Article  CAS  PubMed  Google Scholar 

  • Sawyer, C. H. and J. W. Everett: Cholinesterases in rat tissues and the site of serum non-specific cholinesterase production. Amer. J. Physiol 148, 675–683 (1947).

    CAS  PubMed  Google Scholar 

  • Scaife, J. F.: Stability of cholinesterase of the electric eel. Nature (Loud.) 183, 541 (1959).

    Article  CAS  Google Scholar 

  • Schaefer, H.: Luber das normale Verhalten der Cholinesterase im Blut. Pflügers Arch. ges. Physiol. 249, 405–430 (1947).

    CAS  Google Scholar 

  • Schümmelfeder, N.: Untersuchungen über Cholinesterase im Blut nach experimentellen Schädigungen. I. Mitteilung. Bestimmungsmethode und Einfluß von Narkose, operativen Eingriffen und Blutentnahmen. Naunyn-Schmiedeberg’s Arch. exp. Path. Pharmak. 204, 454–465 (1947).

    Google Scholar 

  • Scoz, G., and C. Cattaneo: Determination of cholinesterase activity in blood with electrometric titration (Italian). Enzymologia 4, 157–162 (1937).

    CAS  Google Scholar 

  • Serlin, I., and G. C. Cotzias: Microdiffusion of acetic acid as an assay for acetylcholinesterase. J. biol. Chem. 215, 263–268 (1955).

    CAS  PubMed  Google Scholar 

  • Shibata, S., and H. Takahashi: A simple procedure for the estimation of serum cholinesterase by means of comparator with phenol red as indicator. Bull. Yamaguchi med. School 1, 188–197 (1953).

    Google Scholar 

  • Skorepa, J.: Electrophoretic mobility of plasma esterase after injection of heparin. Clin. chim. Acta 1, 499–500 (1956).

    CAS  Google Scholar 

  • Simonart, A.: Contribution à l’étude des propriétés pharmacologique des dérivés de la choline. Rev. belge Sci. méd. 5, 73–112 (1933).

    Google Scholar 

  • Sleisenger, M. H., T. P. Almy, H. Gilder and G. Perle: Colorimetric determination of serum cholinesterase. its value in hepatic and biliary tract diseases. J. clin. Invest. 32, 466–472 (1953).

    Article  CAS  PubMed  Google Scholar 

  • Smallman, B. N., and L. S. Wolfe: The effect of salts on the estimation of cholinesterase activity. Enzymologia 17, 133–144 (1955).

    Google Scholar 

  • Snyder, H. H., C. D. Snyder and L. D. Bunch: Serum cholinesterase levels in surgical patients. A preliminary report. Amer. Surg. 17, 959–980 (1951).

    CAS  Google Scholar 

  • Stedman, E., and E. Stedman: The relative choline-esterase activities of serum and corpuscles from the blood of certain species. Biochem. J. 29, 2107–2111 (1935).

    CAS  PubMed  Google Scholar 

  • E. Stedman, and E. Stedman and L. H. Easson: Choline-esterase. An enzyme present in the blood-serum of the horse. Biochem. J. 26, 2056–2066 (1932).

    CAS  PubMed  Google Scholar 

  • E. Stedman, and E. Stedman and L. H. Easson and A. C. White: A comparison of the choline-esterase activities of the blood-sera from various species. Biochem. J. 27, 1055–1060 (1933).

    CAS  PubMed  Google Scholar 

  • Steowee, D.: Properties of insect cholinesterase. Acta physiol. pharmacol. neerl. 1, 336–337 (1950).

    Google Scholar 

  • Studies Steowee, D.: on cholinesterase in insects. Physiol. comp. oecol. 2, 241–247 (1951).

    Google Scholar 

  • Straus, O. H., and A. Goldstein: Zone behavior of enzymes. Illustrated by the effect of dissociation constant and dilution on the system cholinesterase-physostigmine. J. gen. Physiol. 26, 559–585 (1943).

    Article  CAS  PubMed  Google Scholar 

  • Strehler, E., u. H. Meyer: Die Plasma-Cholinesterase bei Gesunden und Kranken. Helv. med. Acta 19, 555–577 (1952).

    CAS  Google Scholar 

  • Strelitz, F.: Studies on cholinesterase. 4. Purification of pseudo-cholinesterase from horse serum. Biochem. J. 38, 86–88 (1944).

    CAS  PubMed  Google Scholar 

  • Stumpf, C.: Methoden zur Bestimmung der Cholinesteraseaktivität im Blut. Z. Vitamin-, Hormon-u. Fermentforsch. 8, 36–48 (1956).

    CAS  Google Scholar 

  • Sturge, L. M., and V. P. Whittaker: The esterases of horse blood. 1. The specificity of horse plasma cholinesterase and ali-esterase. Biochem. J. 47, 518–525 (1950).

    CAS  PubMed  Google Scholar 

  • D. M. Surgenor, and D. Ellis: Preparation and properties of serum and plasma proteins. Plasma cholinesterase. J. Amer. chem. Soc. 76, 6049–6051 (1954).

    Article  CAS  Google Scholar 

  • D. M. Surgenor, and D. Ellis L. E. Strong, H. L. Taylor, R. S. Gordon and D. M. Gibson: The separation of choline esterase, mucoprotein, and metal-combining protein into subfractions of human plasma. J. Amer. them. Soc. 71, 1223–1229 (1949).

    CAS  Google Scholar 

  • Tabacinick, I. I. A.: A rapid, spectrophotometric assay of purified cholinesterase. Biochim. biophys. Acta 21, 580–581 (1956).

    Google Scholar 

  • Tabacinick, I. I. A. J. Mershon, M. E. Grelis and A. A. RUBIN: A rapid spectrophotometric assay of cholinesterase inhibitors. Arch. int. Pharmacodyn. 114, 351–353 (1958).

    Google Scholar 

  • Takahashi, H.: Studies on serum cholinesterase. I. A method for the estimation of serum cholinesterase activity which is useful in the routine work of clinical laboratory. Bull. Yamaguchi med. School 3, 155–165 (1956).

    Google Scholar 

  • Takahashi, H. and S. SHIBATA: A simple method for the serum cholinesterase determination applicable to routine examination (Japanese). Igaku to Seibutsugaku 20, 96–98 (1951); Chem. Abstr. 46, 9647 (1953).

    Google Scholar 

  • Tamai, A.: On the cholinesterase of dog liver. J. Japan. biochem. Soc. 22, 29–32 (1950); J. Biochem. (Tokyo) 38, June, I II (1951).

    Google Scholar 

  • Tam’eelin, L.-E.: An electrometric method for the determination of cholinesterase activity. I. Apparatus and cholinesterase in human blood. Scand. J. clin. Lab. Invest. 5, 267–270 (1953).

    Article  Google Scholar 

  • Tam’eelin, L.-E.: Choline esters. Substrates and inhibitors of cholinesterases. Svensk kem. T. 70, 157–181 (1958).

    Google Scholar 

  • Tam’eelin, L.-E. and H. Löw: Calibration of an electrometric method for the determination of cholinesterase activity. Acta them. scand. 5, 322–323 (1951).

    Article  Google Scholar 

  • Tam’eelin, L.-E. and B. Strindberg: Cholinesterase activity determined with an electrometric method. Acta chem. scand. 6, 1041–1047 (1952).

    Article  Google Scholar 

  • Tauber, H.: A method for the preparation of a stable brain fraction containing acetylcholinesterase. J. Amer. chem. Soc. 75, 326–328 (1953).

    Article  CAS  Google Scholar 

  • Thompson, R. H. S.: Cholinesterases. Brit. med. Bull. 9, 138–141 (1953).

    CAS  Google Scholar 

  • Thompson, R. H. S.: Cholinesterases and anti-cholinesterases. In Lectures on the Scientific Basis of Medicine, vol. II, 165–180. London The Athlone Press 1954.

    Google Scholar 

  • Tobias, J. M., J. J. Kollros and J. Savit: Acetylcholine and related substances in the cockroach, fly, and crayfish and the effect of DDT. J. cell. comp. Physiol. 28, 159–182 (1946).

    Article  CAS  Google Scholar 

  • Todrick, A.: The inhibition of cholinesterases by antagonists of acetylcholine and histamine. Brit. J. Pharmacol. 9, 76–83 (1954).

    Google Scholar 

  • Todrick, A. K. P. Fellowes and J. P. Rutland: The effect of alcohols on cholinesterase. Biochem. J. 48, 360–368 (1951).

    Google Scholar 

  • Togni, G. P., u. O. Meier: Über das Verhalten der Serumcholinesterase des Pferdes bei der Papierelektrophorese. Experientia (Basel) 9, 106–107 (1953).

    Article  CAS  Google Scholar 

  • Toscm, G.: Chromatographic and electrophoretic studies on cholinesterases of nerve tissue (Italian). R. C. Ist. sup. Sanità 21, 1077–1096 (1958).

    Google Scholar 

  • Toscm, G.: Biochemical study of brain microsomes. Exp. Cell. Res. 16, 232–255 (1959).

    Article  Google Scholar 

  • Underhay, E. E.: The hydrolysis of indoxyl esters by esterases of human blood. Biochem. J. 66, 383–390 (1957).

    CAS  PubMed  Google Scholar 

  • Vahlquist, B.: On the esterase activity of human blood plasma. Skand. Arch. Physiol. 72, 133–160 (1935).

    Article  CAS  Google Scholar 

  • Varga, E., J. Szigeti u. E. Kiss: Hydrolyse des Azetylcholins in Gegenwart von gereinigtem Myosin. Acta physiol. Acad. Sci. hung. 5, 383–392 (1954).

    CAS  Google Scholar 

  • Vincent, D.: Acétylcholine, cholinestérases et anticholinestérases. Prod. pharm. 10, 17–24, 85–97 (1955).

    Google Scholar 

  • Vincent, D. et R. LAGREU: Action comparée de qulques dérivés alcaloidiques puriques (caféine, théobromine, théophylline et théophylline-éthylène-diamine) sur les cholinestérases. C. R. Soc. Biol. (Paris) 144, 925–927 (1950).

    CAS  Google Scholar 

  • Vincent, D. et G. Segonzag: Adaptation pratique de la méthode de Hestrin au dosage de la pseudocholinestérase sérique. Ann. Biol. clin. 16, 227–232 (1958).

    CAS  Google Scholar 

  • Vincent, D. et G. Segonzag et J. DE PRAT: La cholinestérase du sérum, son dosage. Intérêt clinique de son étude. Ann. Biol. clin. 2, 35 (1944).

    Google Scholar 

  • Walop, J. N.: Studies on acetylcholine in the crustacean central nervous system. Arch. int. Pharmacodyn. 59, 145–156 (1951).

    CAS  Google Scholar 

  • Walop, J. N. and L. M. Boot: Studies on cholinesterase in Carcinus maenas. Biochim. biophys. Acta 4, 566–571 (1950).

    CAS  Google Scholar 

  • Warringa, M. G. P. J., and J. A. Cohen: Purification of cholinesterase from ox red cells. Biochim. biophys. Acta 16, 300 (1955).

    CAS  Google Scholar 

  • Wetstone, H. J., R. Tennant and B. V. White: Studies of cholinesterase activity. I. Serum cholinesterase, methods and normal values. Gastroenterology 33, 41–49 (1957).

    CAS  PubMed  Google Scholar 

  • Whittaker, V. P.: The specificity of pigeon-brain cholinesterase. Biochem. J. 44, P 46—P 47 (1949).

    Google Scholar 

  • Whittaker, V. P. Specificity, mode of action and distribution of cholinesterases. Physiol. Rev. 31, 312–343 (1951).

    CAS  PubMed  Google Scholar 

  • Whittaker, V. P. The specificity of pigeon brain aceto-cholinesterase. Biochem. J. 54, 660–664 (1953).

    CAS  PubMed  Google Scholar 

  • Whittaker, V. P. and S. Wijesundera: The separation of esters of choline by filter-paper chromatography. Biochem. J. 51, 348–351 (1952).

    CAS  PubMed  Google Scholar 

  • Williams, M. W., J. P. Frawley, H. N. Fuyat and J. R. Blake: Modification of the Michel electrometric technique for dog and rat blood cholinesterase. J. Ass. agric. Chem. (Wash.) 40, 1118–1120 (1957).

    CAS  Google Scholar 

  • Wilson, I. B.: Mechanism of enzymic hydrolysis. I. Role of the acide group in the esteratic site of acetylcholinesterase. Biochim biophys. Acta 7, 466–470 (1951).

    CAS  Google Scholar 

  • Wilson, I. B.: The mechanism of enzyme hydrolysis studies with acetylcholinesterase. In. W. D. MCELROY and B. GLASS, Eds., The Mechanism of Enzyme Action, 642–657. Baltimore Johns Hopkins Press 1954.

    Google Scholar 

  • Wilson, I. B.: Promotion of acetylcholinesterase activity by the anionic site. Disc. Faraday Soc. 20, 119–125 (1955).

    Article  Google Scholar 

  • Wilson, I. B.: Acetylcholinesterase. In. P. D. BOYER, H. LARDY and K. MYRBACK, Eds., The Enzymes, 2nd ed., vol. 4, 501–520. New York. Academic Press 1960.

    Google Scholar 

  • Wilson, I. B. and F. Bergmann: Acetylcholinesterase. VIII. Dissociation constants of the active groups. J. biol. Chem. 186, 683–692 (1950).

    CAS  PubMed  Google Scholar 

  • Wolfe, L. S., and B. N. Smallman: The properties of cholinesterase from insects. J. cell. comp. Physiol. 48, 215–235 (1956).

    Article  CAS  Google Scholar 

  • Wolfsie, J. H.: Blood cholinesterase activity. Practical consideration in routine testing programs. Arch. indust. Hlth 16, 403–410 (1957).

    CAS  Google Scholar 

  • Wolfsie, J. H. and G. D. Winter: Statistical analysis of normal human red blood cell and plasma cholinesterase activity values. Arch. indust. Hyg. 6, 43–49 (1952); 7, 352 (1953).

    Google Scholar 

  • Wolfsie, J. H. and G. D. Winter: Bromothymol blue screening test. Value for determination of blood cholinesterase activity. Arch. indust. Hyg. 9, 396–401 (1954).

    CAS  Google Scholar 

  • Zajicek, J., and E. Zeuthen: Quantitative determination of cholinesterase activity in individual cells. Exp. Cell. Res. 11, 568–579 (1956).

    Article  CAS  PubMed  Google Scholar 

  • Zarr, F. J.: Eine modifizierte Warburg-Apparatur. Hoppe-Seylers Z. physiol. Chem. 307, 36–41 (1957).

    Google Scholar 

  • Zavaleta, O.: Blood cholinesterase in apparently healthy subjects. Laboratorio (Granada) 20, 301–324 (1955).

    Google Scholar 

  • Zeller, E. A.: Enzymes of snake venoms and their biological significance. Advanc. Enzymol. 8, 459–495 (1948).

    CAS  Google Scholar 

  • Zeller, E. A.: Über die Cholinesterase der Schlangengifte. 5. Mitteilung über die Biochemie der tierischen Gifte. Helv. chim. Acta 32, 94–105 (1949).

    CAS  Google Scholar 

  • Zeller, E. A. u. A. Bissegger: Über die Cholinesterase des Gehirns und der Erythrocyten. 3. Mitteilung über die Beeinflussung von Fermentreaktionen durch Chemotherapeutica und Pharmaka. Helv. chim. Acta 26, 1619–1630 (1943).

    CAS  Google Scholar 

  • Zeller, E. A. u. A. Bissegger G. A. Fleisher u R A Mcnaughton: Non-choline esters as substrates of e-cholinesterase (“true” cholinesterase). Fed. Proc. 8, 268 (1949).

    Google Scholar 

  • Zeller, E. A. u. A. Bissegger and J. S. SCHWEPPE: New substrates for cholinesterases. Proc. Soc. exp. Biol. (N. Y.) 71, 526–529 (1949).

    Article  CAS  Google Scholar 

  • Zeller, E. A. u. A. Bissegger u. D. C. UTZ: Über die Spezifität der Cholinesterase der Schlangengifte. 6. Mitteilung über über die Biochemie tierischer Gifte. Helv. chim. Acta 32, 338–347 (1949).

    CAS  Google Scholar 

  • Zittle, C. A., E. S. Dellamonica and J. H. Custer: Purification of human red cell acetyl-cholinesterase. Arch. Biochem. 48, 43–49 (1954).

    Article  CAS  PubMed  Google Scholar 

  • Zittle, C. A., E. S. Dellamonica and J. H. Custer and R. Krikorian: Purification of human red cell acetylcholinesterase by electrophoresis, ultracentrifugation and gradient extraction. Arch. Biochem. 56, 469–475 (1955).

    Article  CAS  PubMed  Google Scholar 

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  1. Klas-Bertil Augustinsson
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  1. Department of Pharmacology, Schools of Medicine, University of Pennsylvania, Philadelphia 4, Pa., USA

    George B. Koelle Ph.D., M.D. (Professor and Chairman) (Professor and Chairman)

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Augustinsson, KB. (1963). Classification and Comparative Enzymology of the Cholinesterases and Methods for their Determination. In: Koelle, G.B. (eds) Cholinesterases and Anticholinesterase Agents. Handbook of Experimental Pharmacology, vol 15. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-99875-1_4

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