Abstract
<h2>Abstract</h2> Fibrillar collagen suspensions and neutral salt soluble collagen were investigated with regard to their platelet aggregating activity. The activity of fibrillar suspensions was highly dependent on the method of preparation and was observed to increase with the fineness of dispersion. Monodisperse tropocollagen was found not to aggregate platelets. However, aggregating activity developed after multimerizing the molecules by incubation at 37° C. At this stage no fibrils could be detected by measuring the opacity at 400 nm. It is proposed that the triple helix is an insufficient structure for promoting platelet aggregation; multimers of tropocollagen are required to induce this platelet reaction. Evidence for a close correlation between fibril precipitation and development of aggregating activity is presented. Treatment of soluble collagen with galactose oxidase was shown to interfere with multimerization and consequently to lead to a delayed development of aggregating activity. Enzyme treated and control collagen showed similar aggregating activities after multimerization at 37° C. Treatment of fibrillar collagen with galactose oxidase produced no loss in aggregating activity as compared to control collagen.
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