Purification and partial amino acid sequence of osteogenin, a protein initiating bone differentiation

F. P. Luyten, N. S. Cunningham, S. Ma, N. Muthukumaran, R. G. Hammonds, W. B. Nevins, W. I. Wood, A Hari Reddi

Research output: Contribution to journalArticle

327 Scopus citations

Abstract

Osteogenin was purified from bovine bone matrix and its activity monitored by an in vivo bone induction assay. The purification method utilized extraction of the bone-inducing activity with 6 M urea, followed by chromatography on heparin-Sepharose, hydroxyapatite, and Sephacryl S-200. Active fractions were further purified by preparative sodium dodecyl sulfate gel electrophoresis without reduction. Osteogenin activity was localized in a zone between 30 and 40 kDa. The amino acid sequences of a number of tryptic peptides of the gel-eluted material were determined. Reduction and alkylation of purified osteogenin in 7 M guanidine hydrochloride resulted in the total loss of biological activity. Sodium dodecyl sulfate gel electrophoresis under reducing conditions revealed a broad band with an apparent molecular mass of 22 kDa.

Original languageEnglish (US)
Pages (from-to)13377-13380
Number of pages4
JournalJournal of Biological Chemistry
Volume264
Issue number23
StatePublished - 1989
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry

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    Luyten, F. P., Cunningham, N. S., Ma, S., Muthukumaran, N., Hammonds, R. G., Nevins, W. B., Wood, W. I., & Reddi, A. H. (1989). Purification and partial amino acid sequence of osteogenin, a protein initiating bone differentiation. Journal of Biological Chemistry, 264(23), 13377-13380.