Abstract
Rabbit atropinesterase and cocainesterase were studied by starch gel electrophoresis. The enzymes are localized in a region of the gels anodal to the albumins (prealbumin esterases). In this region, three groups of esterase zones (S, F, and D) can be distinguished. The S and F zones are almost exclusively responsible for the hydrolysis of cocaine and atropine, respectively. There is an interdependence of the S, F, and D zones: the activity of zone D depends on the presence of the three F zones, whereas these F zones are found only in combination with the three S zones. α-Naphthylacetate as a substrate reveals six different phenotypes; two of these phenotypes are shown to be composed of two subtypes when a supplementary staining procedure is executed. Atropinesterase and cocainesterase are classified as carboxylesterases (E.C. 3.1.1.1.) with a rather wide specificity for both aliphatic and aromatic esters. The α-naphthol esters are split better than the corresponding β-naphthol esters. Naphthol esters with an acyl side-chain of three carbon atoms are hydrolyzed optimally by the enzymes.
This is a preview of subscription content, log in via an institution to check access.
Similar content being viewed by others
References
Aldridge, W. H. (1971). The nature of the reaction of organophosphorus compounds and carbamates with esterases. Bull. World Health Org. 4425.
Augustinsson, K. B. (1958). Electrophoretic separation and classification of blood plasma esterase. Nature 1811786.
Augustinsson, K. B. (1961). Multiple forms of esterase in vertebrate blood plasma. Ann. N.Y. Acad. Sci. 94844.
Choudhury, S. A., and Lundy, A. M. (1971). Differential inhibition of esterase isozymes by organophosphorus compounds. J. Histochem. Cytochem. 19390.
Dixon, M., and Webb, E. (1967). Enzymes, 2nd ed., Longmans, London.
Ecobichon, D. J. (1970). Characterization of the esterases of canine serum. Can. J. Biochem. Physiol. 481359.
Estabrooks, L., and Schiff, R. (1972). Esterase isozymes from rabbit synovial fluids of normal and artificial joints. J. Histochem. Cytochem. 20211.
Gomori, G. (1955). Histochemistry of human esterases. J. Histochem. Cytochem. 3479.
Grunder, A. A., Sartore, C., and Stormont, C. (1965). Genetic variation in red cell esterases of rabbits. Genetics 521345.
Harris, H. (1969). Genes and isozymes. Proc. Roy. Soc. Lond. Ser. B 1741.
Holmes, R. S., and Masters, C. J. (1967). The developmental multiplicity and isozyme status of cavian esterases. Biochim. Biophys. Acta 132379.
Hunter, R. L., and Markert, C. L. (1957). Histochemical demonstration of enzyme separated by zone electrophoresis in starch gels. Science 1251294.
Junge, W., and Krisch, K. (1971). Subunit weight and N-terminal groups of liver and kidney carboxylesterase (EC. 3.1.1.1). FEBS Letters 12189.
Krisch, B., and Krisch, K. (1972). Electron microscopy of pig liver carboxylesterase. FEBS Letters 24146.
Krisch, K. (1973). Molecular and catalytic properties of unspecific carboxylesterases (EC. 3.1.1.1). Physiol. Chem. 3543.
Margolis, F., and Feigelson, P. (1963). Purification and characterization of a genetically determined rabbit serum esterase. J. Biol. Chem. 2382620.
Markert, C. L., and Hunter, R. L. (1959). The distribution of esterases in mouse tissues. J. Histochem. Cytochem. 742.
National Academy of Sciences U.S.A.-National Research Council Report (1969). Application of metabolic data to the evaluation of drugs. Clin. Pharmacol. Ther. 10607.
Ogita, Z. (1968). Genetic control of isozymes. Ann. N.Y. Acad. Sci. 151243.
Sargent, J. R. (1969). Methods in Zone Electrophoresis, BDH-Chemicals, Poole.
Schiff, R. (1970). The biochemical genetics of rabbit erythrocyte esterases: Histochemical classification. J. Histochem. Cytochem. 18709.
Schiff, R., and Stormont, C. (1970). The biochemical genetics of rabbit erythrocyte esterases: Two new esterase loci. Biochem. Genet. 411.
Smithies, O. (1959). An improved procedure for starch-gel electrophoresis: Further variations in the serum proteins of normal individuals. Biochem. J. 71585.
Stormont, C., and Suzuki, Y. (1970). Atropinesterase and cocainesterase of rabbit serum: Localization of the enzyme activity in isozymes. Science 167200.
van Zutphen, L. F. M. (1972). Qualitative and quantitative detection of atropinesterase and cocainesterase in two breeds of rabbits. Enzymologia 42201.
van Zutphen, L. F. M. (1973). Substrate specificity and inhibitor sensitivity of rabbit cocainesterase. IRCS Medical Science (73-7) 3-1-16.
van Zutphen, L. F. M. (1974). Serum esterase genetics in rabbits. II. Genetic analysis of the prealbumin esterase system, including atropinesterase and cocainesterase polymorphism. Biochem. Genet. 12327.
Webb, E. C. (1964). The nomenclature of multiple enzyme forms. Experientia 20592.
Wilkinson, J. H. (1970). Isozymes, 2nd ed., Chapman and Hall, London.
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
van Zutphen, L.F.M. Serum esterase genetics in rabbits. I. Phenotypic variation of the prealbumin esterases and classification of atropinesterase and cocainesterase. Biochem Genet 12, 309–326 (1974). https://doi.org/10.1007/BF00485951
Received:
Revised:
Issue Date:
DOI: https://doi.org/10.1007/BF00485951