Abstract
SummaryUtilizing an improved isolation procedure, interstitial connective tissue from cardiac muscle was isolated in yields of approximately 6% of the dry muscle mass. The amino acid composition of intact cardiac collagen was markedly different from that of skin collagen. Yields of acid-soluble tropocollagen from bovine and rat cardiac collagen were only 0.1 to 1% of that obtained from rat skin collagen. Disc gel patterns and carboxymethyl cellulose chromatograms of soluble cardiac collagen revealed a marked reduction in α and β-components and large quantities of higher molecular weight aggregates. These results suggest the presence of an extensive interchain cross-linking network in cardiac collagen.
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Schedule a callMore From: Proceedings of the Society for Experimental Biology and Medicine. Society for Experimental Biology and Medicine (New York, N.Y.)
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