Two different types of interstitial collagen in the muscle layer of the marine polychaete Hermodice sp.

Abstract

Two different interstitial collagens were isolated from the muscle layer of the marine polychaete worm Hermodice sp. (Annelida). Collagens were solubilized after limited pepsin digestion and fractionated by a differential sale precipitation procedure. Both types of interstitial collagen (Hermodice collagens A and B) appear to be homotrimers with subunit compositions (alpha A)(3) and (alpha B)(3), respectively. Both types of subunits alpha A and alpha B migrate in SDS-PAGE between the alpha 1(I) and alpha 2(I) subunits of type I collagen with an apparent molecular weight of 100,000. SLS crystallites from Hermodice collagen A exhibited a band pattern similar to that of vertebrate type I collagen, whereas collagen B showed a very different band pattern, suggesting substantial sequence differences between the two types of collagen. The amino acid composition of Hermodice collagens A and B showed marked differences

notwithstanding, both collagens fit the pattern of interstitial collagens. The A:B ratio is 1.9, as determined from the amino acid analysis. (C) 1997 Elsevier Science Inc.