在胰凝乳蛋白酶原和α-胰凝乳蛋白酶的温度控制转变过程中甲硫氨酸残基的构象状态。 - Suppr | 超能文献

The conformational state of methionine residues in the temperature-controlled transition of chymotrypsinogen and -chymotrypsin.

作者信息

Wasi S, Hofmann T

出版信息

Can J Biochem. 1973 Jun;51(6):797-805. doi: 10.1139/o73-099.

DOI:10.1139/o73-099

Abstract

摘要

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The conformational state of methionine residues in the temperature-controlled transition of chymotrypsinogen and -chymotrypsin.在胰凝乳蛋白酶原和α-胰凝乳蛋白酶的温度控制转变过程中甲硫氨酸残基的构象状态。

Can J Biochem. 1973 Jun;51(6):797-805. doi: 10.1139/o73-099.

2

A calorimetric study of the chymotrypsinogen family of proteins.蛋白质胰凝乳蛋白酶原家族的量热研究。

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Electron paramagnetic resonance probing of macromolecules: a comparison of structure-function relationships in chymotrypsinogen, -chymotrypsin and anhydrochymotrypsin.

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Oxidation of methionine residues in proteins of activated human neutrophils.活化的人中性粒细胞蛋白质中蛋氨酸残基的氧化

Proc Natl Acad Sci U S A. 1983 Dec;80(23):7160-4. doi: 10.1073/pnas.80.23.7160.

2

The effect of temperature on the individual stages of the hydrolysis of non-specific-p-nitrophenol esters by alpha-chymotrypsin.温度对α-胰凝乳蛋白酶水解非特异性对硝基苯酚酯各个阶段的影响。

Biochem J. 1977 Jan 1;161(1):83-92. doi: 10.1042/bj1610083.