The isolation of anionic phosphoproteins from bovine cortical bone Via the periodate solubilization of bone collagen

Adrian Shuttleworth*, Arthur Veis

*Corresponding author for this work

Research output: Contribution to journalArticle

39 Scopus citations

Abstract

Purified, decalcified bovine bone matrix was partially solubilized by prolonged oxidative degradation with sodium metaperiodate. Fractionation of a portion of the solubilized bone matrix on DEAE-cellulose led to the isolation of two anionic components (0.55 and 0.75 M NaCl elutions). Analysis showed each component to be a protein characterized by a high content of aspartic and glutamic acids, serine and glycine. A substantial portion of the serine was present as serine phosphate in both compounds. Galactosamine was found in the component eluted with 0.55 M NaCl and this fraction probably represents degraded protein-polysaccharide. The other component, eluted with 0.75 M NaCl, contained no hexosamine but did contain hydroxylysine. Disc electrophoresis showed this component to be similar to a phosphoprotein isolated from dentin collagen. The possible relationship between the bone and dentin phosphoproteins and their role in mineralization is discussed.

Original languageEnglish (US)
Pages (from-to)414-420
Number of pages7
JournalBBA - Protein Structure
Volume257
Issue number2
DOIs
StatePublished - Feb 29 1972

ASJC Scopus subject areas

  • Medicine(all)

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