DIRECT INVOLVEMENT OF THE C-TERMINAL EXTREMITY OF PANCREATIC LIPASE (403-449) IN COLIPASE BINDING

被引：16

作者：

CHAILLAN, C ^{[1
]}

KERFELEC, B ^{[1
]}

FOGLIZZO, E ^{[1
]}

CHAPUS, C ^{[1
]}

机构：

[1] CNRS,CTR BIOCHIM & BIOL MOLEC,31 CHEMIN J AIGUIER,F-13402 MARSEILLE 9,FRANCE

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1992年 / 184卷 / 01期

关键词：

D O I：

10.1016/0006-291X(92)91179-T

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：

After a selective cleavage of a lipase/colipase cross-linked complex, the colipase has been shown to be bound to a 5 kDa lipase fragment identified as the C-terminal extremity of the chain extending from residue 403 to the C-terminus (Cys 449). The colipase binding site on lipase is therefore localized in a restricted contact area. Moreover, from sequence comparison of lipase from various species, an acidic residue, Glu 440, is likely to be involved in ion pairing with colipase. © 1992.

引用

页码：206 / 211

页数：6

共 36 条

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