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The kinetics of the two-step interaction of chymotrypsin with proflavin.

作者信息

Havsteen B H

出版信息

J Biol Chem. 1967 Feb 25;242(4):769-71.

PMID:6018237
Abstract
摘要

相似文献

1
The kinetics of the two-step interaction of chymotrypsin with proflavin.胰凝乳蛋白酶与原黄素两步相互作用的动力学
J Biol Chem. 1967 Feb 25;242(4):769-71.
2
On the interaction of the active side of alpha-chymotrypsin with chromophores: proflavin binding and enzyme conformation during catalysis.关于α-糜蛋白酶活性位点与发色团的相互作用：催化过程中的原黄素结合与酶构象
J Mol Biol. 1966 Jul;18(3):405-20. doi: 10.1016/s0022-2836(66)80033-5.
3
Transient formation of a complex between alpha-chymotrypsin, proflavin, and tosylarginine methyl ester (TAME).
Can J Biochem. 1972 Mar;50(3):257-60. doi: 10.1139/o72-036.
4
Activation of chymotrypsin catalyted hydrolyses by 9-aminoacridine.
Biochem Biophys Res Commun. 1966 May 3;23(3):246-51. doi: 10.1016/0006-291x(66)90536-5.
5
[Adjustment of the substrate as rate-determining step in the enzymatic cleavage of esters and amides by chymotrypsin A].[通过胰凝乳蛋白酶A对酯和酰胺进行酶促裂解时作为速率决定步骤的底物调整]
Hoppe Seylers Z Physiol Chem. 1969 Dec;350(12):1501-12.
6
A change in specificity of chymotrypsin caused by chemical modification of methionine residues.
J Biol Chem. 1966 Jun 10;241(11):2687-93.
7
Calorimetric investigations of the binding of inhibitors to alpha-chymotrypsin. I. The enthalpy of dilution of alpha-chymotrypsin and of proflavin, and the enthalpy of binding of indole, N-acetyl-D-tryptophan, and proflavin to alpha-chymotrypsin.
Biochemistry. 1969 Dec;8(12):4910-7. doi: 10.1021/bi00840a039.
8
Interaction of delta-chymotrypsin with proflavine.δ-胰凝乳蛋白酶与原黄素的相互作用。
Can J Biochem. 1971 Jan;49(1):28-31. doi: 10.1139/o71-005.
9
Proflavin-chymotrypsin interaction: high pressure temperature-jump studies.
Arch Int Physiol Biochim. 1974 Feb;82(1):205.
10
Spectroscopic investigation of the interaction of -chymotrypsin with proflavin.
Mol Biol. 1971 Sep-Oct;5(5):567-72.

引用本文的文献

1
Protonation linked equilibria and apparent affinity constants: the thermodynamic profile of the alpha-chymotrypsin-proflavin interaction.质子化相关平衡与表观亲和常数：α-糜蛋白酶-原黄素相互作用的热力学概况
Eur Biophys J. 2007 Dec;37(1):11-8. doi: 10.1007/s00249-007-0148-0. Epub 2007 Apr 19.
2
Low dielectric response in enzyme active site.酶活性位点的低介电响应
Proc Natl Acad Sci U S A. 2000 Feb 29;97(5):2081-6. doi: 10.1073/pnas.050316997.
3
The time-dependent specific interation of 4-(4'-aminophenylazo)phenylarsonic acid with subtilsins.
4-（4'-氨基苯偶氮）苯胂酸与枯草杆菌蛋白酶的时间依赖性特异性相互作用
Proc Natl Acad Sci U S A. 1968 Mar;59(3):996-1002. doi: 10.1073/pnas.59.3.996.
4
Acylation of alpha-chymotrypsin by oxygen and sulfur esters of specific substrates: kinetic evidence for a tetrahedral intermediate.特定底物的氧酯和硫酯对α-糜蛋白酶的酰化作用：四面体中间体的动力学证据
Proc Natl Acad Sci U S A. 1974 May;71(5):1643-7. doi: 10.1073/pnas.71.5.1643.
5
[Structural flexibility and enzyme function].[结构灵活性与酶功能]
Naturwissenschaften. 1969 May;56(5):232-7. doi: 10.1007/BF00633916.
6
General method for exact evaluation of parameters of the elementary steps of coupled reactions. Invariant analysis.耦合反应基元步骤参数精确评估的通用方法。不变量分析。
Biochem J. 1985 Dec 15;232(3):791-7. doi: 10.1042/bj2320791.