TY - JOUR
T1 - The Nature of Covalent Complexes of Phosphoproteins with Collagen in the Bovine Dentin Matrix
AU - Curley-Joseph, Jean
AU - Veis, Arthur
PY - 1979/6
Y1 - 1979/6
N2 - The bovine dentin matrix still contains some non-collagenous proteins after thorough extraction and decalcification. These have been obtained following digestion of the matrix by cyanogen bromide. Peptides containing non-collagenous portions were isolated by chromatography on diethylaminoethyl cellulose columns and fractionated on hydroxyapatite columns. Several fractions were obtained. The principal component was a complex between a highly-phosphorylated serine-aspartic acid-rich protein and a collagen peptide. These collagenous and non-collagenous moieties could not be separated from each other even under highly dissociative solvent conditions. After digestion with collagenase, the resulting phosphoprotein fraction still contained a few residues of hydroxyproline and hydroxylysine, and an enhanced content of pro-line, compared to the equivalent directly extractable phosphophoryn of the matrix. These data were interpreted as indicating that the phosphophoryn which is not extractable in 0.5M ethylenediaminetetraacetic acid is in fact covalently bound to some specific section of the matrix collagen. The covalent modification of the collagen matrix with highly acidic phosphoproteins may have an important role in the mineralization process.
AB - The bovine dentin matrix still contains some non-collagenous proteins after thorough extraction and decalcification. These have been obtained following digestion of the matrix by cyanogen bromide. Peptides containing non-collagenous portions were isolated by chromatography on diethylaminoethyl cellulose columns and fractionated on hydroxyapatite columns. Several fractions were obtained. The principal component was a complex between a highly-phosphorylated serine-aspartic acid-rich protein and a collagen peptide. These collagenous and non-collagenous moieties could not be separated from each other even under highly dissociative solvent conditions. After digestion with collagenase, the resulting phosphoprotein fraction still contained a few residues of hydroxyproline and hydroxylysine, and an enhanced content of pro-line, compared to the equivalent directly extractable phosphophoryn of the matrix. These data were interpreted as indicating that the phosphophoryn which is not extractable in 0.5M ethylenediaminetetraacetic acid is in fact covalently bound to some specific section of the matrix collagen. The covalent modification of the collagen matrix with highly acidic phosphoproteins may have an important role in the mineralization process.
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U2 - 10.1177/00220345790580061201
DO - 10.1177/00220345790580061201
M3 - Article
C2 - 221556
AN - SCOPUS:0018732131
SN - 0022-0345
VL - 58
SP - 1625
EP - 1633
JO - Journal of Dental Research
JF - Journal of Dental Research
IS - 6
ER -