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 language | English (US) |
|---|---|
| Pages (from-to) | 13377-13380 |
| Number of pages | 4 |
| Journal | Journal of Biological Chemistry |
| Volume | 264 |
| Issue number | 23 |
| State | Published - 1989 |
| Externally published | Yes |
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ASJC Scopus subject areas
- Biochemistry
Cite this
Purification and partial amino acid sequence of osteogenin, a protein initiating bone differentiation. / Luyten, F. P.; Cunningham, N. S.; Ma, S.; Muthukumaran, N.; Hammonds, R. G.; Nevins, W. B.; Wood, W. I.; Reddi, A Hari.
In: Journal of Biological Chemistry, Vol. 264, No. 23, 1989, p. 13377-13380.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Purification and partial amino acid sequence of osteogenin, a protein initiating bone differentiation
AU - Luyten, F. P.
AU - Cunningham, N. S.
AU - Ma, S.
AU - Muthukumaran, N.
AU - Hammonds, R. G.
AU - Nevins, W. B.
AU - Wood, W. I.
AU - Reddi, A Hari
PY - 1989
Y1 - 1989
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=0024356071&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0024356071&partnerID=8YFLogxK
M3 - Article
C2 - 2547759
AN - SCOPUS:0024356071
VL - 264
SP - 13377
EP - 13380
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
SN - 0021-9258
IS - 23
ER -