Primary structure of the heparin-binding site of type V collagen.
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.
Yaoi
Y
Y
Biology Division, National Cancer Center Research Institute, Tokyo, Japan.
Hashimoto
K
K
Koitabashi
H
H
Takahara
K
K
Ito
M
M
Kato
I
I
D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D002417:Cattle; D002846:Chromatography, Affinity; D002851:Chromatography, High Pressure Liquid; D003094:Collagen / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*; D006493:Heparin / Q000378:metabolism*; D006801:Humans; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000302:isolation & purification; D010447:Peptide Hydrolases; D010449:Peptide Mapping
D010446:Peptide Fragments; D006493:Heparin; D003094:Collagen; D010447:Peptide Hydrolases