Title: Purification and partial amino acid sequence of osteogenin, a protein initiating bone differentiation
Authors: Luyten, F P ×
Cunningham, N S
Ma, S
Muthukumaran, N
Hammonds, R G
Nevins, W B
Woods, W I
Reddi, A H #
Issue Date: 12-Sep-1989
Series Title: Journal of Biological Chemistry vol:264 issue:23 pages:13377-80
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.
ISSN: 0021-9258
Publication status: published
KU Leuven publication type: IT
Appears in Collections:Rheumatology Section (-)
× corresponding author
# (joint) last author

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