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 journalArticlepeer-review

332 Scopus citations


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
Issue number23
StatePublished - 1989
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry


Dive into the research topics of 'Purification and partial amino acid sequence of osteogenin, a protein initiating bone differentiation'. Together they form a unique fingerprint.

Cite this