Metal-catalyzed photooxidation of histidine in human growth hormone

被引：40

作者：

Chang, SH ^{[1
]}

Teshima, GM ^{[1
]}

Milby, T ^{[1
]}

GilleceCastro, B ^{[1
]}

CanovaDavis, E ^{[1
]}

机构：

[1] GENENTECH INC, San Francisco, CA 94080 USA

来源：

ANALYTICAL BIOCHEMISTRY | 1997年 / 244卷 / 02期

关键词：

D O I：

10.1006/abio.1996.9899

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

Reports on nonenzymatic oxidation of human growth hormone (hGH) have been previously limited to methionyl residues (Met(14) and Met(125)). We report on the oxidation of a histidyl residue in hGH treated with intense light. The photooxidation process is predominately site-specific to histidine at position 21, which forms a cation-binding site along with His(18) and Glu(174). This site binds metal ions and, under intense light, catalyzes the oxidation of His(21). Products are formed by the addition of one, two, or three atoms of oxygen to the histidyl residue. (C) 1997 Academic Press

引用

页码：221 / 227

页数：7

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