AMINO-ACID-COMPOSITION AND N-TERMINAL SEQUENCE OF PURIFIED CYSTINE BINDING-PROTEIN OF ESCHERICHIA-COLI

被引：21
|
作者：
BUTLER, JD
LEVIN, SW
FACCHIANO, A
MIELE, L
MUKHERJEE, AB
机构：
[1] WALTER REED ARMY MED CTR,DEPT PEDIAT,EXCEPT FAMILY MEMBER PROGRAM,WASHINGTON,DC 20307
[2] NICHHD,HUMAN GENET BRANCH,DEV GENET SECT,BETHESDA,MD 20892
来源：
LIFE SCIENCES | 1993年 / 52卷 / 14期
关键词：
D O I：
10.1016/0024-3205(93)90103-A
中图分类号：
R-3 [医学研究方法]; R3 [基础医学];
学科分类号：
1001 ;
摘要：
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.
引用
收藏
页码：1209 / 1215
页数：7
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