DISULFIDE ARRANGEMENT OF HUMAN INSULIN-LIKE GROWTH FACTOR-I DERIVED FROM YEAST AND PLASMA

被引：7

作者：

AXELSSON, K ^{[1
]}

JOHANSSON, S ^{[1
]}

EKETORP, G ^{[1
]}

ZAZZI, H ^{[1
]}

HEMMENDORF, B ^{[1
]}

GELLERFORS, P ^{[1
]}

机构：

[1] KABI PHARMACIA,PEPTIDE HORMONES,LINDHAGENSG 133,S-11287 STOCKHOLM,SWEDEN

来源：

EUROPEAN JOURNAL OF BIOCHEMISTRY | 1992年 / 206卷 / 03期

关键词：

D O I：

10.1111/j.1432-1033.1992.tb17010.x

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：

The disulfide arrangement of yeast derived human insulin-like growth factor I (yIGF-I) was determined using a combination of Staphylococcus aureus V8 protease mapping, fast-atom-bombardment mass spectrometry as well as amino acid sequence and composition analysis. Three disulfide bridges were found between the following cysteine residues: Cys6-Cys48, Cys47-Cys52 and Cys18-Cys61. IGF-I isolated from human plasma (pIGF-I) was found to have an identical dilsufide configuration. A yeast-derived isomeric form of IGF-I (yisoIGF-I) exhibited an altered disulfide arrangement: Cys6-Cys47, Cys48-Cys52 and Cys18-Cys61. Radioreceptor analysis of pIGF-I and yIGF-I showed high specific activity, 20000 U/mg. However, yisoIGF-I demonstrated a severely reduced ability to bind to the IGF-I receptor (19%) and was less potent in provoking a mitogenic response in Balb/C 3T3 fibroblasts (50% at doses 10-100 ng/ml). The data demonstrate the importance of correct disulfide arrangement in IGF-I for full biological activity.

引用

页码：987 / 994

页数：8

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