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http://hdl.handle.net/11154/2867
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Title: | Two different types of interstitial collagen in the muscle layer of the marine polychaete Hermodice sp. |
Authors: | Garza, G Torre-Blanco, Alfonso Miguel |
Issue Date: | 1997 |
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. |
URI: | http://hdl.handle.net/11154/2867 |
ISSN: | 3050491 |
Appears in Collections: | Departamento de Biología Celular
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