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J. Biol. Chem., Vol. 264, Issue 23, 13377-13380, 08, 1989
FP Luyten, NS Cunningham, S Ma, N Muthukumaran, RG Hammonds, WB Nevins, WI Woods and AH Reddi
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.
Purification and partial amino acid sequence of osteogenin, a protein initiating bone differentiation
Bone Cell Biology Section, National Institute of Dental Research, Bethesda, Maryland 20892.
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