title: Properties of chymotrypsin bound covalently to dextran.
abstract: The kinetic properties dextran-chymotrypsin conjugate were studied by means of low molecular weight substrates. It was found that KM, kcat and kcat/KM of dextran chymotrypsin for the hydrolysis of benzoyl-L-tyrosine-ethyl-ester did not differ substantially from those of the free enzyme. However, the data found for kcat of dextran-chymotrypsin and free chymotrypsin assayed for the hydrolysis of three tripeptidyl-p-nitroanilide D-Arg-Val-Trp-pNA, D-Arg-Val-Tyr-pNA, Z-Phe-Pro-Phe-pNA, were definitely different. The inhibition of the modified chymotrypsin with soybean trypsin inhibitor was found to be less pronounced than that with the free enzyme. The effect of potassium and magnesium salts on the inactivation of both enzymes was also studied. The effect of dextran matrix on the catalytic properties and the conformational stability of modified chymotrypsin is discussed.
authors: Department of Biotechnology, Higher Institute of Chemical Technology, Sofia, Bulgaria.
authors: T P
authors: TP
authors: Zlateva
authors: M
authors: M
authors: Krysteva
authors: Z
authors: Z
authors: Balajthy
authors: P
authors: P
authors: Elödi
mesh_terms: D000818:Animals; D002417:Cattle; D002918:Chymotrypsin / Q000378:metabolism*; D003911:Dextrans / Q000378:metabolism*; D004791:Enzyme Inhibitors; D006868:Hydrolysis; D007700:Kinetics; D013379:Substrate Specificity; D013997:Time Factors; D014361:Trypsin Inhibitors / Q000378:metabolism
chemical_list: D003911:Dextrans; D004791:Enzyme Inhibitors; D014361:Trypsin Inhibitors; D002918:Chymotrypsin