A numerical method for acquisition and processing of steady-state kinetic data contained in an entire progression curve. Application to the study of -chymotrypsin-catalyzed hydrolysis. - Suppr | 超能文献

A numerical method for acquisition and processing of steady-state kinetic data contained in an entire progression curve. Application to the study of -chymotrypsin-catalyzed hydrolysis.

作者信息

Bizzozero S, Kaiser A W, Dutler H

出版信息

Eur J Biochem. 1973 Mar 1;33(2):292-300. doi: 10.1111/j.1432-1033.1973.tb02683.x.

DOI:10.1111/j.1432-1033.1973.tb02683.x

Abstract

摘要

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A numerical method for acquisition and processing of steady-state kinetic data contained in an entire progression curve. Application to the study of -chymotrypsin-catalyzed hydrolysis.

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Chymotrypsin-catalyzed phenyl ester hydrolysis. Evidence for electrophilic assistance on carbonyl oxygen.胰凝乳蛋白酶催化的苯基酯水解。羰基氧上亲电辅助作用的证据。

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Investigations of the chymotrypsin-catalyzed hydrolysis of specific substrates. V. Determination of pre-steady state kinetic parameters for specific substrate esters by stopped flow techniques.胰凝乳蛋白酶催化特定底物水解的研究。V. 用停流技术测定特定底物酯的稳态前动力学参数。

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Kinetic investigation of the alpha-chymotrypsin-catalyzed hydrolysis of peptide-ester substrates. The relationship between the structure of the peptide moiety and reactivity.α-胰凝乳蛋白酶催化肽酯底物水解的动力学研究。肽部分结构与反应活性之间的关系。

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Microb Ecol. 1977 Jun;3(2):107-18. doi: 10.1007/BF02010400.

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Expressions of the Michaelis-Menten equation when studying enzyme reactions in a variable-volume medium.在可变体积介质中研究酶反应时米氏方程的表达式。

Biochem J. 1974 Dec;143(3):771-3. doi: 10.1042/bj1430771.