Abstract
Abstract The denatured α1 chain from chick skin collagen, at a concentration of 0.1%, causes human platelets to aggregate. This activity appears to reside in only one of the chick skin α1 cyanogen bromide peptides (α1-CB5). Inhibition and periodate oxidation studies implicate the carbohydrate moiety of the chick skin α1-CB5 glycopeptide as one of its structural determinants. Evidence is also presented that native, triple helical collagen (tropocollagen) possesses an independent plateletaggregating activity in which its carbohydrate moiety is not involved. The quaternary structure of collagen fibrils appears to possess a third independent platelet-aggregating activity for which the carbohydrate moiety seems to be required.
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