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大肠杆菌纯化胱氨酸结合蛋白的氨基酸组成及N端序列

Amino acid composition and N-terminal sequence of purified cystine binding protein of Escherichia coli.

作者信息

Butler J D, Levin S W, Facchiano A, Miele L, Mukherjee A B

机构信息

Unit on Genetic Diseases Involving Sulfur Metabolism, National Institute of Child Health and Human Development, Bethesda, Maryland 20982.

出版信息

Life Sci. 1993;52(14):1209-15. doi: 10.1016/0024-3205(93)90103-a.

Abstract

Cystine Binding Protein (CBP), a commercially available crude protein extract obtained by osmotic shock of Escherichia coli (E. coli), was studied to characterize further its cystine binding properties and to elucidate its cystine transport activity. We report here the amino acid composition, the N-terminal amino acid sequence analysis and some binding characteristics of the purified cystine binding component of CBP. A search of the Swiss-Prot version 20 data base revealed that this sequence is unique.

摘要

胱氨酸结合蛋白(CBP)是一种通过对大肠杆菌进行渗透休克获得的市售粗蛋白提取物,对其胱氨酸结合特性进行了进一步研究,并阐明其胱氨酸转运活性。我们在此报告了CBP纯化的胱氨酸结合成分的氨基酸组成、N端氨基酸序列分析及一些结合特性。对瑞士蛋白质数据库20版的搜索显示该序列是独一无二的。

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