Presence of lysinoalanine and histidinoalanine in bovine dentin phosphoprotein.
Trypsin digestion and successive calcium-induced precipitation of the insoluble bovine dentin matrix effectively separated the collagen and phosphoprotein fractions which were firmly associated together in this material. Amino acid analysis by four different systems revealed that the lysinoalanine and histidinoalanine, which had been previously reported to occur in the human dentin collagen, were concentrated in the phosphoprotein fraction but were not present in the collagen fraction. Furthermore, it was found that the free-type phosphoprotein which was isolated from EDTA extract of dentin powder also contained both "cross-linking" amino acids. The results indicated the both "cross-links" distributed within the dentin phosphoprotein and were not likely to contribute the unique stability of dentin collagen.
D000818:Animals; D001857:Bone Matrix / Q000378:metabolism; D002417:Cattle; D003804:Dentin / Q000378:metabolism*; D004151:Dipeptides / Q000378:metabolism*; D008239:Lysine / Q000031:analogs & derivatives*; D008241:Lysinoalanine / Q000378:metabolism*; D010750:Phosphoproteins / Q000378:metabolism*
D004151:Dipeptides; D010750:Phosphoproteins; C034124:histidinoalanine; D008241:Lysinoalanine; D008239:Lysine