Abstract
The molecular species of collagen in the muscle layer of the ascidian Halocynthia roretzi was examined by biochemical techniques. Two types of collagen which showed distinct patterns from each other on SDS-PAGE were isolated from the pepsin-solubilized collagen by differential salt precipitation and phosphocellulose column chromatography. They were demonstrated to be genetically distinct from each other by peptide mapping and by amino acid analysis. These results indicate that at least two molecular species of collagen are present in the muscle layer of the ascidian.
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