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Primary structure of the heparin-binding site of type V collagen

Authors :
Kazuhiko Takahara
Ikunoshin Kato
Manabu Ito
Hashimoto Kahoko
Yoshihito Yaoi
Hiroyuki Koitabashi
Source :
Biochimica et biophysica acta. 1035(2)
Publication Year :
1990

Abstract

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 alpha 1(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 the heparin-binding site of type V collagen.

Details

ISSN :
00063002
Volume :
1035
Issue :
2
Database :
OpenAIRE
Journal :
Biochimica et biophysica acta
Accession number :
edsair.doi.dedup.....1c8b5df2576c71d665930ab7ca28cd14