Skip to main content
SpringerLink
Log in

Variation in rates of activity and inhibition of serum cholinesterase among anthropoid primates

  • Published:
International Journal of Primatology Aims and scope Submit manuscript

Abstract

Cholinesterase activity in the plasma of five hominoid and five cercopithecoid species was measured and characterized by profiles of inhibition by dibucaine and sodium fluoride. Chimpanzees and gorillas strongly resemble humans, and differ from other hominoids and cercopithecoids, in patterns of dibucaine and fluoride resistance and relative activity toward various thio esters. “Silent” cholinesterase phenotypes of probable veterinary significance, and analogous to a rare human variant, are apparently normal in some catarrhine species and are present as a polymorphism among orangutans and lion-tailed macaques.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Log in via an institution

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Institutional subscriptions

Similar content being viewed by others

References

  • Altland, K., and Goedde, H. W. (1970). Heterogeneity in the silent gene phenotype of pseudocholinesterase of human serum.Biochem. Genet. 4: 321–338.

    Article  PubMed  CAS  Google Scholar 

  • Altland, K., Goedde, H. W., Held, K., Jensen, M., Munsch, H., and Solem, E. (1971). New biochemical and immunological data on quantitative and qualitative variability of human pseudocholinesterase.Humangenetik 14: 56–60.

    Article  PubMed  CAS  Google Scholar 

  • Augustinsson, K. B. (1948). Cholinesterases. A study of comparative enzymology.Acta physiol. Scand. 15: Suppl. 52.

    Google Scholar 

  • Augustinsson, K. B. (1959). Electrophoretic studies on blood plasma esterases. I. Mammalian plasmata.Acta chem. Scand. 13: 571–592.

    CAS  Google Scholar 

  • Augustinsson, K. B. (1961). Multiple forms of esterase in vertebrate blood plasma.Ann. N. Y. Acad. Sci. 94: 844–860.

    Article  CAS  Google Scholar 

  • Bourne, J. C., Collier, H. O., and Somers, G. F. (1952). Succinylcholine (succinoylcholine): Muscle relaxant of short action.Lancet 1: 1225–1229.

    Article  PubMed  CAS  Google Scholar 

  • Breed, R. T., and Jolly, C. J. (1987). Identification and phyletic distribution of the plasma esterases of some anthropoid primates.Int. J. Primatol. 8: 331–350.

    Google Scholar 

  • Brown, S. S., Kalow, W., Piltz, W., Whittaker, M., and Woronick, C. L. (1981). The plasma cholinesterases: A new perspective.Adv. clin. Chem. 22: 1–123.

    PubMed  CAS  Google Scholar 

  • Ellman, G. L., Coutney, D., Andres, V., and Featherstone, R. (1961). A new and rapid colorimetric determination of acetylcholinesterase activity.Biochem. Pharmacol. 7: 88–95.

    Article  PubMed  CAS  Google Scholar 

  • Froede, H. (1971). Acetylcholinesterase. In Boyer, P. D. (ed.),The Enzymes, Academic Press, New York, Vol. 5, pp. 87–114.

    Google Scholar 

  • Goedde, H. W., Held, K., and Altland, K. (1968). Hydrolysis of succinyldicholine and succinylmonocholine in human serum.Mol. Pharmacol. 4: 274.

    PubMed  CAS  Google Scholar 

  • Hanssen, G. H. (1957). Cholinesterases and muscle relaxants. II. Blood and muscle cholinesterase activities in domestic animals.Acta pharmacol. toxicol. 13: 142–154.

    Article  Google Scholar 

  • Harris, H., and Whittaker, M. (1961). Differential inhibition of human serum cholinesterase with fluoride: Recognition of two new phenotypes.Nature (London) 191: 496–498.

    Article  CAS  Google Scholar 

  • Harris, H., and Whittaker, M. (1962). The serum cholinesterase variants. A study of 22 families selected via the “intermediate” phenotype.Ann. hum. Genet. 27: 53–58.

    Article  Google Scholar 

  • Harris, H., and Whittaker, M. (1963). Differential inhibition of “usual” and “atypical” cholinesterase by sodium chloride and sodium fluoride.Ann. hum. Genet. 27: 53–58.

    Article  PubMed  CAS  Google Scholar 

  • Harris, H., Hopkinson, D., and Robson, E. (1962). Two-dimensional electrophoresis of pseudocholinesterase components in normal human serum.Nature (London) 196: 1296.

    Article  CAS  Google Scholar 

  • Harris, H., Hopkinson, D., Robson, E., and Whittaker, M. (1963). Genetical studies on a new variant of pseudocholinesterase detected by electrophoresis.Ann. hum. Genet. 26: 359–382.

    Article  PubMed  CAS  Google Scholar 

  • Heibronn, E. (1965). Action of fluoride on cholinesterase. I. On the mechanism of inhibition.Acta chem. Scand. 19: 1333–1346.

    Google Scholar 

  • Hobbiger, F., and Peck, A. W. (1971). Relative importance of the enzymatic hydrolysis of suxamethonium in plasma and tissue: studies in cats.Br. J. Pharmacol. 43: 341–348.

    PubMed  CAS  Google Scholar 

  • Kalow, W. (1956). The relation of plasma cholinesterases to response to clinical doses of succinylcholine.Can. anesth. Soc. J. 3: 22–30.

    Article  Google Scholar 

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

    Article  Google Scholar 

  • Kalow, W., and Genest, K. (1957). A method for the detection of atypical forms of human serum cholinesterase. Determination of dibucaine numbers.Can. J. Biochem. Physiol. 35: 339–346.

    PubMed  CAS  Google Scholar 

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

    PubMed  CAS  Google Scholar 

  • Kalow, W., and Maycut, M. O. (1956). The interaction between cholinesterases and a series of local anaesthetics.J. Pharmacol. 116: 418.

    CAS  Google Scholar 

  • Kalow, W., and Staron, N. (1957). On the distribution and inheritance of atypical forms of human serum cholinesterase, as indicated by dibucaine numbers.Can. J. Biochem. Physiol. 35: 1305–1320.

    PubMed  CAS  Google Scholar 

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

    PubMed  CAS  Google Scholar 

  • Kattamis, C., Davies, D., and Lehmann, H. (1967). The silent serum cholinesterase gene.Acta genet. 17: 299.

    Article  PubMed  CAS  Google Scholar 

  • King, A. W., and Jolly, C. J. (1983). Serogenetic analysis and conservation of the liontailed macaque. In Heltne, P. (ed.),The Liontailed Macaque, Status and Conservation (Monogr. Primatol. 7), Karger, Basel, pp. 195–219.

    Google Scholar 

  • Krupka, R. M. (1966). Fluoride inhibition of actylcholinesterase.Mol. Pharmacol. 2: 558–569.

    PubMed  CAS  Google Scholar 

  • La Du, B. (1971). Plasma esterase activities and the metabolism of drugs with ester groups.Ann. N. Y. Acad. Sci. 179: 684–694.

    Article  PubMed  CAS  Google Scholar 

  • La Du, B. N., Mandel, H. G., and Way, E. L. (1971).Fundamentals of Drug Metabolism and Drug Disposition, Williams and Wilkins, Baltimore.

    Google Scholar 

  • Liddell, J., Lehman, H., and Silk, E. (1962). A “silent” gene of pseudocholinesterase.Nature (London) 193: 561.

    Article  CAS  Google Scholar 

  • Lockridge, O., and La Du, B. (1978). Comparison of atypical and usual human serum cholinesterase. Purification, number of active sites, substrate affinity, and turnover number.J. biol. Chem. 253: 361–366.

    PubMed  CAS  Google Scholar 

  • Lockridge, O., and La Du, B. (1982). Loss of the interchain disulfide peptide and dissociation of the tetramer following limited proteolysis of native human serum cholinesterase.J. biol. Chem. 257: 12012–12018.

    PubMed  CAS  Google Scholar 

  • Lockridge, O., Eckerson, H. W., and La Du, B. (1979). Interchain disulfide bonds and subunit organization in human serum cholinesterase.J. biol. Chem. 254: 8324–8330.

    PubMed  CAS  Google Scholar 

  • Muensch, H., Goedde, H. W., and Yoshida, A. (1976). Human serum cholinesterase subunits and number of active sites of the major component.Eur. J. Biochem. 70: 217–223.

    Article  PubMed  CAS  Google Scholar 

  • Muensch, H., Yoshida, A., Altland, K., Jensen, W., and Goedde, H. W. (1978). Structural difference at the active site of dibucaine resistant variant of human plasma cholinesterase.Am. J. hum. Genet. 30: 302–307.

    PubMed  CAS  Google Scholar 

  • Orgell, W. H. (1963). Inhibition of human plasma cholinesterasein vitro by alkaloids, glycosides and other natural substances.Lloydia 26: 34–43.

    Google Scholar 

  • Simpson, N. E., and Kalow, W. (1964). The “silent” gene for serum cholinesterase.Am. J. hum. Genet. 16: 180.

    PubMed  CAS  Google Scholar 

  • Stewart, D. J., Inaba, T., Tang, B. K., and Kalow, W. (1977). Hydrolysis of cocaine in human plasma by cholinesterase.Life Sci. 20: 1557–1563.

    Article  PubMed  CAS  Google Scholar 

  • Turner, T. R. (1981). Blood protein variation in a population of vervet monkeys.Am. J. Phys. Anthrop. 55: 225–232.

    Article  Google Scholar 

  • Van Dyke, C., and Byck, R. (1982). Cocaine.Sci. Am. 246: 128–141.

    Article  PubMed  Google Scholar 

  • Van Dyke, C., Barash, P. G., Jatlow, P., and Byck, R. (1976). Cocaine: Plasma concentrations after intranasal application in man.Science 191: 859–861.

    Article  PubMed  Google Scholar 

  • van Zutphen, L. F. M. (1972). Qualitative and quantitative detection of atropinesterase and cocainesterase in two breeds of rabbits.Enzymologia 42: 201–218.

    Google Scholar 

  • Weber, H. (1966). Rasche und einfache Ultramikromethode zur Bestimmung der Serumcholinesterase.Dtsch. med. Wschr. 91: 1927–1932.

    Article  PubMed  CAS  Google Scholar 

  • Wright, P. G. (1981). Species variation in plasma cholinesterase activity.Comp. Biochem. Physiol. 70: 289–291.

    CAS  Google Scholar 

Download references

Author information

Authors and Affiliations

  1. Department of Anthropology, New York University, 10003, New York, New York

    Ria T. Breed & Clifford J. Jolly

Authors
  1. Ria T. Breed
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. Clifford J. Jolly
    View author publications

    You can also search for this author in PubMed Google Scholar

Rights and permissions

Reprints and permissions

About this article

Cite this article

Breed, R.T., Jolly, C.J. Variation in rates of activity and inhibition of serum cholinesterase among anthropoid primates. Int J Primatol 9, 97–112 (1988). https://doi.org/10.1007/BF02735731

Download citation

  • Received:

  • Revised:

  • Issue Date:

  • DOI: https://doi.org/10.1007/BF02735731

Key words

Search

Navigation