Cross-Linking Characteristics of Cardiac Muscle Collagen

Abstract

Summary

Utilizing 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.