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001-es BibID:	BIBFORM078153
035-os BibID:	(PMID)2470217
Első szerző:	Zlateva, T. P.
Cím:	Properties of chymotrypsin bound covalently to dextran / Zlateva, T. P., Krysteva, M., Balajthy, Z., Elödi, P.
Dátum:	1988
Megjegyzések:	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.
Tárgyszavak:	Természettudományok Biológiai tudományok idegen nyelvű folyóiratközlemény hazai lapban
Megjelenés:	Acta Biochimica et Biophysica Hungarica. - 23 : 3-4 (1988), p. 225-230. -
További szerzők:	Krysteva, M. Balajthy Zoltán (1957-) (biokémikus, sejtbiológus) Elődi Pál (1927-2002) (biokémikus)
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