Abstract
Comparative enzymologic study of catalytic properties of cholinesterase (ChE) in blood serum of the American mink Mustela vison Schr. has revealed several peculiarities of this enzyme. First, using the method of substrate–inhibitor analysis, homogeneity of the ChE preparation has been established, i.e. only one ChE has been found in mink serum. Second, the rate of acetylcholine hydrolysis was higher than of thiocholine substrates, among which propionylthiocholine was hydrolyzed at the highest rate. Third, propionylthiocholine had the highest V/K M value that reflects to a degree affinity of the substrate to enzyme. Fourth, the phenomenon of “substrate inhibition,” which is not inherent for mammalian serum cholinesterases, is revealed and kinetically analyzed. Fifth, study of inhibitory specificity has not revealed differences of the mink serum ChE from other serum ChE.
This is a preview of subscription content, log in via an institution to check access.
Similar content being viewed by others
REFERENCES
Berestov, V.A. and Kozhevnikova, L.K., Fermenty krovi pushnykh zverei (Enzymes in Blood of Fur Animals), Leningrad, 1981.
Sadykov, A.S., Rozengart, E.V., Abduvakhabov, A.A., and Aslanov, Kh.A., Kholinesterazy. Aktivnyi tsentr i mekhanizm deistviya (Cholinesterases. Active Center and Action Mechanism), Tashkent, 1976.
Brestkin, A.P., Kuznetsova, L.P., Moralev, S.N., Rozengart, E.V., and Epshtein, L.M., Kholinesterazy nazemnykh zhivotnykh i gidrobiontov (Cholinesterases of Terrestrial Animals and Hydrobionts), Vladivostok, 1997.
Ocherki po fiziologii pushnykh zverei (Assays on Physiology of Fur Animals), Berestov, V.A., Ed., Leningrad, 1987.
Ellman, G.L., Courtney, K.D., Andres, V., and Featherstone, R.M., A New and Rapid Colorimetric Determination of Acetylcholinesterase Activity, Biochem. Pharmacol., 1961, vol. 7, pp. 88–95.
Moralev, S.N. and Rozengart, E.V., “Substrate Inhibition” Is One of Aspects of Substrate Specificity of Vertebrate and Invertebrate Cholinesterases, Zh. Evol. Biokhim. Fiziol., 2001, vol. 37, pp. 358–373.
Radic, Z., Duran, R., Vellom, D.C., and Quinn, D.M., Site of Fasciculin Interaction with Acetylcholinesterase, J. Biol. Chem., 1994, vol. 269, pp. 11 233–11 239.
Rozengart, E.V., Khovanskikh, A.E., and Epshtein, L.M., Study of Homogeneity of Cholinesterase Activity in the Nervous Tissue of Squids by Method of Substrate.Inhibitor Analysis, Zh. Evol. Biokhim. Fiziol., 1994, vol. 30, pp. 15–22.
Brestkin, A.P., Zhukovskii, Yu. G., and Sipenkova, T.M., Hydrolysis of Choline and Thiocholine Esters by Cholinesterases, Biokhimiya, 1974, vol. 39, pp. 13–18.
Brestkin, A.P., Zhukovskii, Yu.G., and Fartseiger, N.L., Catalytic Properties of Cholinesterases from the Brain and Blood Serum of the Pigeon Columba livia, Zh. Evol. Biokhim. Fiziol., 1983, vol. 19, pp. 138–143.
Brestkin, A.P. and Parkhomenko, T.V., Substrate Specificity of Partially Purified Cholinesterase from Chicken Blood Serum, Biokhimiya, 1971, vol. 36, pp. 950–955.
Rozengart, E.V., Substrate.Inhibitor Analysis of Cholinesterase of the Pacific Gastropod Mollusc Neptunea eulimata, Zh. Evol. Biokhim. Fiziol., 2001, vol. 37, pp. 165–169.
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Rozengart, E.V., Khovanskikh, A.E., Basova, N.E. et al. Comparative Enzymologic Study of Catalytic Properties of Blood Serum Cholinesterase of the American Mink Mustela vison . Journal of Evolutionary Biochemistry and Physiology 38, 401–406 (2002). https://doi.org/10.1023/A:1021145602100
Issue Date:
DOI: https://doi.org/10.1023/A:1021145602100