Yaoi Y, Hashimoto K, Koitabashi H, Takahara K, Ito M, Kato I
Biology Division, National Cancer Center Research Institute, Tokyo, Japan.
Biochim Biophys Acta. 1990 Aug 17;1035(2):139-45. doi: 10.1016/0304-4165(90)90108-9.
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.
通过肝素亲和色谱法以及与[35S]肝素的结合研究，检测了I型、II型、III型、IV型和V型胶原蛋白与肝素的结合能力。在生理pH值和离子强度下，只有V型胶原蛋白能与肝素结合。I型和II型胶原蛋白对肝素的亲和力高于III型和IV型，但在生理离子强度下不与肝素柱结合。V型胶原蛋白的肝素结合位点位于α1(V)链的一个30 kDa溴化氰片段中，并测定了该片段的氨基酸序列。30 kDa片段包含一簇碱性氨基酸残基，该碱性结构域内的酶切大大降低了所得肽段的肝素结合活性。因此，这个碱性区域可能是V型胶原蛋白的肝素结合位点。
