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  • Title: Systematic purification of free and matrix-bound phosphophoryns of bovine dentin: presence of matrix-bound phosphophoryn as a distinct molecular entity.
    Author: Fujisawa R, Takagi T, Kuboki Y, Sasaki S.
    Journal: Calcif Tissue Int; 1984 Mar; 36(2):239-42. PubMed ID: 6430506.
    Abstract:
    Free and matrix-bound phosphophoryns, both highly phosphorylated proteins in dentin, were prepared from EDTA extract and CNBr-digests of bovine dentin. The two components were purified by DEAE-cellulose, SP-Sephadex, and gel filtration chromatography. The matrix-bound component was eluted as a distinct peak from the free component in the above chromatographic systems. Amino acid composition of the purified matrix-bound component indicated that this component consisted of phosphophoryn and collagen in the ratio of 2:3 based on the number of the residues. The matrix-bound component could not be reconstituted by mixing phosphophoryn with collagen CNBr peptides. Artificial crosslink products of free phosphophoryn and collagen CNBr-peptides by the carbodiimide method showed similar properties to the physiological matrix-bound phosphophoryn. The bond between phosphophoryn and collagen of the matrix-bound component is assumed to be a covalent crosslink.
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