Chemical nature of collagen in the placoid-scale dentine of the blue shark, Prionace glauca L.
The dentine fraction was obtained from powdered placoid scales by differential density-flotation, and demineralized with 0.5 M EDTA. Monomeric alpha 1 and alpha 2 chains of collagen were extracted from the residual organic matrix, and the two alpha chains purified by chromatography. The two alpha chains were also isolated from shark-skin collagen. The corresponding alpha chains from shark dentine and skin collagens resembled each other closely in chromatographic and electrophoretic behaviour and in their CNBr-peptide maps but differed from calf-skin alpha chains. The differences in the chemical composition between shark dentine and skin were due only to post-translational modification (hydroxylation and phosphorylation), indicating that the collagens are of the same type. The hydroxylation of prolyl and lysyl residues occurred more in the dentine alpha chains than in the skin chains. Among the four alpha chains, the phosphate content was the highest in the alpha 2 chain of the dentine collagen. These differences in hydroxylation and phosphorylation have been observed among alpha chains of mammalian mineralized and unmineralized tissues. The preferential dimerization to form alpha 1-alpha 2, characteristic of shark-skin collagen, was not observed in the dentine collagen. Other dimers were hardly detectable in the latter.
D000818:Animals; D055598:Chemical Phenomena; D002621:Chemistry; D003094:Collagen; D003804:Dentin / Q000032:analysis*; D012754:Sharks / Q000378:metabolism*; D012867:Skin / Q000032:analysis
D003094:Collagen