Solubilization and characterization of Chondrosia reniformis sponge collagen.
Chondrosia reniformis sponge collagen, insoluble in its native form, was solubilized by chemical modification of lysyl residues. The solubilized sponge collagen had the same amino acid composition as insoluble collagen and the helicoidal tertiary structure was found by negative Cotton effect to be the same as in native vertebrate collagens. Achromobacter iophagus collagenase, a collagen specific protease, hydrolyzed the soluble sponge collagen. These experiments confirmed that the protein had the same structure as collagen.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D003094:Collagen / Q000032:analysis* / Q000378:metabolism; D003012:Microbial Collagenase / Q000378:metabolism; D008854:Microscopy, Electron; D011161:Porifera / Q000032:analysis*; D012995:Solubility
D000596:Amino Acids; D003094:Collagen; D003012:Microbial Collagenase