HUMAN INTERLEUKIN-5 EXPRESSED IN ESCHERICHIA-COLI - ASSIGNMENT OF THE DISULFIDE BRIDGES OF THE PURIFIED UNGLYCOSYLATED PROTEIN

被引：21

作者：

PROUDFOOT, AEI

DAVIES, JG

TURCATTI, G

WINGFIELD, PT

机构：

[1] UNIV GENEVA,DEPT BIOCHIM MED,CH-1211 GENEVA 4,SWITZERLAND

[2] NIH,PROT EXPRESS LAB,BETHESDA,MD 20892

来源：

FEBS LETTERS | 1991年 / 283卷 / 01期

关键词：

INTERLEUKIN-5; RECOMBINANT DNA TECHNOLOGY; DISULFIDE BOND; PROTEOLYTIC DIGESTION; PEPTIDE MAPPING; HOMODIMERIC SUBUNIT STRUCTURE;

D O I：

10.1016/0014-5793(91)80553-F

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Human interleukin-5 is a homodimer; each subunit contains two cysteine residues that form two inter-subunit disulfide bonds. The topology of the disulfides in recombinant human interleukin-5 produced in Escherichia coli was studied by proteolytic digestion and peptide mapping. Disulfide linked peptides containing cysteine 42 linked to cysteine 84 were isolated. This indicated that cysteines 42 and 84 of one subunit were linked in an antiparallel manner to cysteines 84 and 42 of the other subunit.

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页码：61 / 64

页数：4

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