Robinson J J
Department of Biochemistry Memorial University of Newfoundland, St. John's, Canada.
Comp Biochem Physiol B Biochem Mol Biol. 1997 Jun;117(2):307-13. doi: 10.1016/s0305-0491(97)00092-8.
We report here a biochemical comparison between type 1 rat tail tendon collagen and collagen isolated from sea urchin peristome tissue. The sea urchin collagen consisted of two species of apparent mol masses, 140 and 116 kDa. Amino acid compositional analysis of the 140 and 116 kDa species revealed the presence of hydroxyproline and hydroxylysine as well as a glycine content of 28.1 mol.%. In solubility experiments the rat tail tendon collagen was found to precipitate at sodium chloride concentrations between 1 and 2 M while peristome collagen remained soluble at salt concentrations as high as 4 M. Incubation of the peristome and rat tail tendon collagen preparations with a sea urchin collagenase/gelatinase resulted in cleavage of the former but not the latter collagen. Upon heat denaturation at 60 degrees C, however, the rat tail tendon collagen served as a substrate for the gelatinase. Cyanogen bromide cleavage of rat tail and peristome collagens generated largely unique peptide maps. Collectively, these results suggest that structural differences exist between echinoderm and vertebrate type 1 collagens.
