Identification of aspartic acid 52 as the point of attachment of an affinity label in hen egg white lysozyme. - Suppr | 超能文献

Identification of aspartic acid 52 as the point of attachment of an affinity label in hen egg white lysozyme.

作者信息

Eshdat Y, McKelvy J F, Sharon N

出版信息

J Biol Chem. 1973 Aug 25;248(16):5892-8.

Abstract

摘要

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Identification of aspartic acid 52 as the point of attachment of an affinity label in hen egg white lysozyme.

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Amino acid sequence studies on bobwhite quail egg white lysozyme.关于北美鹑蛋清溶菌酶的氨基酸序列研究。

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Sulfanilation of lysozyme by carbodiimide reaction. Reactivities of individual carboxyl groups.通过碳二亚胺反应对溶菌酶进行磺酰化。单个羧基的反应活性。

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Chemical modification of tyrosyl residues of hen egg-white lysozyme by diisopropylphosphorofluoridate.

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The disulfide bridges of duck egg-white lysozyme II.鸭蛋清溶菌酶II的二硫键

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Disulfide bonds of pepsinogen and pepsin: identification of the disulfide bonds which can be reversibly reduced and reoxidized.胃蛋白酶原和胃蛋白酶的二硫键：可被可逆还原和再氧化的二硫键的鉴定

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Chemical conversion of aspartic acid 52, a catalytic residue in hen egg-white lysozyme, to homoserine.将鸡蛋溶菌酶中的催化残基天冬氨酸52化学转化为高丝氨酸。

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Sulfenylation of tryptophan-62 in hen egg-white lysozyme.鸡蛋清溶菌酶中色氨酸-62的亚磺酰化作用

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引用本文的文献

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Approaches to labeling and identification of active site residues in glycosidases.糖苷酶活性位点残基的标记和鉴定方法。

Protein Sci. 1995 Mar;4(3):361-72. doi: 10.1002/pro.5560040302.

2

Chemical conversion of aspartic acid 52, a catalytic residue in hen egg-white lysozyme, to homoserine.将鸡蛋溶菌酶中的催化残基天冬氨酸52化学转化为高丝氨酸。

Proc Natl Acad Sci U S A. 1974 May;71(5):1658-62. doi: 10.1073/pnas.71.5.1658.