PRIMARY STRUCTURE OF THE HEPARIN-BINDING SITE OF TYPE-V COLLAGEN

被引:45
作者
YAOI, Y
HASHIMOTO, K
KOITABASHI, H
TAKAHARA, K
ITO, M
KATO, I
机构
[1] UNIV TOKYO,COLL ARTS & SCI,DEPT CHEM,TOKYO 113,JAPAN
[2] BIOTECHNOL RES LABS,SHIGA,JAPAN
关键词
Collagen V; Heparin binding site; Primary structure;
D O I
10.1016/0304-4165(90)90108-9
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 abilities of collagens, type I, II, III, IV, and V, to bind heparin were examined by heparin-affinity chromatography and binding studies with [35S]heparin. At a physiological pH and ionic strength, only type V collagen bound to heparin. Collagens type I and II showed higher affinities than types III and IV for heparin, but did not bind to a heparin column at a physiological ionic strength. The heparin binding site of type V collagen was located in a 30 kDa CNBr fragment of the α1(V) chain, and the amino acid sequence of this fragment was determined. The 30 kDa fragment contained a cluster of basic amino acid residues, and enzymatic cleavage within this basic domain greatly reduced the heparin-binding activities of the resulting peptides. Thus this basic region is probably teh heparin-binding site of type V collagen. © 1990.
引用
收藏
页码:139 / 145
页数:7
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