Summary
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1.
After a brief survey of the basic affinity electrophoresis concepts, the usual ways for preparing affinity electrophoresis ligands are examined.
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2.
Then results obtained on cholinesterases are reviewed. This section includes (a) structural and functional investigations on anionic sites, i.e., study of ligand-induced conformational change, organophosphate-induced “aging,” genetic variants, and active-site topology; and (b) characterization of cholinesterase conjugates (hybrid proteins) and glycoinositol phospholipid-anchored cholinesterases.
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3.
The future prospects of affinity electrophoresis, e.g., investigations on the esteratic site and exploration of the carbohydrate moiety, are emphasized in the concluding section.
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References
Amitai, G., Ashani, Y., Shahar, A., Gafni, A., and Silman, I. (1982). Novel pyrene-containing organophosphates as fluorescent probes for studying aging-induced conformational changes in organophosphate-inhibited acetylcholinesterase.Biochemistry 212060–2069.
Arpagaus, M., Kott, M., Vatsis, K. P., Bartels, C. F., La Du, B. N., and Lockridge, O. (1990). Structure of the gene of human butyrylcholinesterase. Evidence for a single copy.Biochemistry 29124–131.
Balny, C., and Masson, P. (1988). Les hautes pressions: outils d'investigation biochimique.Innov. Tech. Biol. Med. 9294–320.
Balny, C., Masson, P., and Travers, F. (1989). Some recent aspects of the use of high-pressure for protein investigations in solution.High Press. Res. 21–28.
Belzunces, L. P., Toutant, J. P., and Bounias, M. (1988). Acetylocholinesterase fromApis mellifera head.Biochem. J. 255463–470.
Bøg-Hansen, T. C., Teisner, B., and Hau, J. (1983). Affinity electrophoresis with special reference to the microheterogeneity of glycoproteins and identification of ligand binding proteins. InModern Methods in Protein Chemistry, Vol. I (H. Tschesche, Ed.), Walter de Gruyter, Berlin, pp. 125–148.
Boschetti, E. (1989). Polyacrylamide derivatives to the service of biospecific separations.J. Biochem. Biophys. Meth. 1921–36.
Eiberg, H., Nielsen, L. S., Klausen, J., Dahlén, M., Kristensen, M., Bisgaard, M. L., Moller, N., and Mohr, J. (1989). Linkage between serum ChE 2 andγ-crystalline gene cluster (CRYG): Assignment to chromosome 2.Clin. Genet. 35313–321.
Ewald, A. H. (1968). Effect of pressure on charge transfer complexes in solution.Trans. Faraday. Soc. 64733–743.
Garner, C. W., Little, G. H., and Pelley, J. W. (1984). Serum cholinesterase inhibition by boronic acids.Biochim. Biophys. Acta 79091–93.
Heremans, K. (1982). High-pressure effects on proteins and other biomolecules.Annu. Rev. Biophys. Bioeng. 111–21.
Hořejši, V. (1979). Some theoretical aspects of affinity electrophoresis.J. Chromatogr. 1781–13.
Hořejši, V., and Tichá, M. (1981). Theory of affinity electrophoresis. Evaluation of the effects of protein multivalency, immobilized ligand heterogeneity and microdistribution and determination of effective concentration of immobilized ligand.J. Chromatogr. 21643–62.
Hořejši, V., and Tichá, M. (1986). Qualitative and quantitative applications of affinity electrophoresis for the study of protein-ligand interaction: A review.J. Chromatogr. 37649–67.
Igloi, G. L., and Kössel, H. (1985). Affinity electrophoresis for monitoring terminal phosphorylation and the presence of queuosine in RNA. Application of polyacrylamide containing a covalently bound boronic acid.Nucl. Acid Res. 136881–6898.
Juul, P. (1968). Human plasma cholinesterase isoenzymes.Clin. Chim. Acta 19205–213.
Kabachnik, M. I., Brestkin, A. P., Godovikov, N. N., Michelson, M. J., Rozengart, E. V., and Rozengart, V. I. (1970). Hydrophobic areas on the active surface of cholinesterases.Pharmacol. Res. 22355–388.
Kalow, W., and Davies, R. O. (1958). The reactivity of various esterase inhibitors towards atypical human serum cholinesterase.Biochem. Pharmacol. 1183–192.
Karnovsky, M. J., and Roots, L. (1964). A “direct-coloring” thiocholine method for cholinesterases.J. Histochem. Cytochem. 12219–221.
La Du, B. N., and Choi, Y. C. (1975). Separation of atypical and usual forms of human serum cholinesterase by affinity chromatography. InIsozymes, 3rd Int. Conf. Isozymes, Vol. 2 (C. L. Markert, Ed.), Academic Press, New York, pp. 877–886.
La Du, B. N. (1989). Identification of the human serum cholinesterase variants using the polymerase chain reaction amplification technique.TiPS 10309–313.
La Du, B. N., Bartels, C., Nogueira, C. P., Arpagaus, M., and Lockridge, O. (1991). Proposed nomenclature for human butyrylcholinesterase genetic variants identified by DNA sequencing.Cell. Mol. Neurobiol. 1179–89.
Lovrien, E. W., Magenis, R. E., Rivas, M. L., Lamvik, N., Rowe, S., Wood, J., and Hemmerling, J. (1978). Serum cholinesterase (E2) linkage analysis possible evidence for localization on chromosome 16.Cytogenet. Cell Genet. 22324–326.
Masson, P. (1985). L'électrophorèse d'affinité des proteines actives. InElectrophorèse et Taxonomie (M. Goyffon, and J. L. D'Hondt, Eds.), Soc. Zool. France, Paris, pp. 73–104.
Masson, P. (1989). A naturally-occurring molecular form of human plasma cholinesterase is an albumin conjugate.Biochim. Biophys. Acta 988258–266.
Masson, P., and Balny, C. (1986). Thermodynamic arguments for temperature induced cryptic conformational change of human plasma cholinesteraseBiochim.Biophys. Acta 874 90–98.
Masson, P., and Goasdoué, J. L. (1986). Evidence that the conformational stability of “aged” organophosphate-inhibited cholinesterase is altered.Biochim. Biophys. Acta 869304–313.
Masson, P., and Marnot, B. (1985). Electrophorèse d'affinité en gel de polyacrylamide. Influence de la concentration du gel sur l'affinité apparente de la cholinestérase pour un ligand de son site anionique.J. Chromatogr. 328135–144.
Masson, P., and Reybaud, J. (1988). Hydrophobic interaction electrophoresis under high hydrostatic pressure: Study of the effects of pressure upon the interaction of serum albumin with a long-chain aliphatic ligand.Electrophoresis 9157–161.
Masson, P., and Vallin, P. (1983). Possibilités d'étude des variantes de la cholinestérase plasmatique humaine par électrophorèse d'affinité.J. Chromatogr. Biomed. Appl. 273289–299.
Masson, P., Sussmilch, A., and Charlet, J. P. (1980). Purification de la butyrylcholinestérase du plasma humain.C.R. Acad. Sci. Paris Ser. D 289537–539.
Masson, P., Privat de Garilhe, A., and Burnat, P. (1982). Formes moleculaires multiples de la butyrylcholinestérase du plasma human. II. Electrophrèse d'affinité des formes C1, C3 et C4.Biochim. Biophys. Acta 701269–284.
Masson, P., Marnot, B., Lombart, J. Y., and Morelis, P. (1984). Etude électrophorétique de la butyrylcholinestérase agée après inhibition par le soman.Biochimie 66235–249.
Masson, P., Chatonnet, A., and Lockridge, O. (1990a). Evidence for a single butyrylcholinesterase gene in individuals carrying the C5 plasma cholinesterase variant (CHE 2).FEBS Lett. 262115–118.
Masson, P., Froment, M. T., Audras, J. C., and Renault, F. (1990b). Molecular characterization of the C5 human plasma cholinesterase variant.Am. Chem. Soc. Symp. Ser. (in press).
Matoušek, V., and Hořejši, V. (1982). Affinity electrophoresis: A theoretical study of the effects of the kinetics of protein-ligand complex formation and dissociation reactions.J. Chromatogr. 254271–290.
Mazza, J. A., Outumuro, P., Moroux, Y., and Boschetti, E. (1989). Polymer design in dye chromatography. InProtein-Dye Interactions (M. A. Vijayalakshmi, and O. Bertrand, Eds.), Elsevier, New York, pp. 126–136.
McGuire, M., Noguera, C., Bartels, C. F., Lightstone, H., Hajra, A., Van des Spek, A. F. L., Lockridge, O., and La Du, B. N. (1989). Identification of the structural mutation responsible for the dibucaine-resistant (atypical) variant form of human serum cholinesterase.Proc. Natl. Acad. Sci. USA 86953–957.
Morild, E. (1981). The theory of pressure effects on enzyme.Adv. Prot. Chem. 3493–166.
Rosenberry, T. L. (1975). Acetylcholinesterase.Adv. Enzymol. 43103–218.
Rosenberry, T. L., Toutant, J. P., Haas, R., and Roberts, W. L. (1989). Identification of glycoinositol phospholipid anchors of membrane proteins.Meth. Cell. Biol. 32231–255.
Shinitzky, M., Dudai, Y., and Silman, I. (1973). Spectral evidence for the presence of tryptophan in the binding site of acetylcholinesterase.FEBS Lett. 30125–128.
Silman, I., and Futerman, A. H. (1987). Mode of attachment of acetylcholinesterase to the surface membrane.Eur. J. Biochem. 17011–22.
Sofeq, H., Zamir, R., Zevin-Sonkin, D., and Zakut, H. (1987). Human cholinesterase genes localized by hybridization to chromosome 3 and 16.Hum. Genet. 77325–328.
Takeo, K. (1987). Affinity electrophoresis. InAdvances in Electrophoresis, Vol. 1 (A. Chrambach, M. J. Dunn, and B. J. Radola, Eds.), VCH, Weinheim, New York, pp. 229–279.
Takeo, K., and Nakamura, S. (1972). Dissociation Constants of glucan phosphorylases of rabbit tissues studied by polyacrylamide gel disc electrophoresis,Arch.Biochem. Biophys. 1531–7.
Toutant, J. P. (1989). Insect acetylcholinesterase: Catalytic properties, tissue distribution and molecular forms,Prog.Neurobiol. 32423–446.
Usdin, E. (1970). Aging. InAnticholinesterase Agents (A. G. Karczmar, E. Usdin, and J. H. Wills, Eds.), Pergamon Press, Oxford, pp. 249–262.
Valentino, R. J., Lockridge, O., Eckerson, H. W., and La Du, B. N. (1981). Prediction of drug sensitivity in individuals with atypical serum cholinesterase based on in vitro biochemical studies.Biochem. Pharmacol. 301643.
Weber, G., and Drickamer, H. G. (1983). The effect of high pressure upon proteins and other biomolecules.Q. Rev. Biophys. 1689–112.
Whittaker, M. (1986).Cholinesterase, Karger, Basel.
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Masson, P. Structural and functional investigations of cholinesterases by means of affinity electrophoresis. Cell Mol Neurobiol 11, 173–189 (1991). https://doi.org/10.1007/BF00712808
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DOI: https://doi.org/10.1007/BF00712808