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The function of collagen carbohydrates in initiation of platelet aggregation

The function of collagen carbohydrates in initiation of platelet aggregation

Thrombosis Research 11(2): 155-162

Periodate modification of collagen [rat tail tendon] can yield a carbohydrate and hydroxylysine-less tropocollagen whose melting temperature is slightly higher than that of unmodified collagen, whose fibril formation in 0.05 M Tris is decreased, and whose fibril formation in plasma is abolished. The periodate-treated tropocollagen can bind to platelets, since displacement by unmodified collagen can be demonstrated, but cannot initiate PRP [platelet rich plasma] aggregation. Fibrils formed from periodate-treated collagen in 0.05 M Tris can initiate aggregation upon addition to PRP. The carbohydrate residues of collagen do play a role in its fibril formation but not in its platelet aggregation.

Accession: 006680349

Download citation: RISBibTeXText

PMID: 198916

DOI: 10.1016/0049-3848(77)90034-2

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