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

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 journal › Article › peer-review

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

ASJC Scopus subject areas

Biochemistry

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

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.",

author = "Luyten, {F. P.} and Cunningham, {N. S.} and S. Ma and N. Muthukumaran and Hammonds, {R. G.} and Nevins, {W. B.} and Wood, {W. I.} and Reddi, {A Hari}",

year = "1989",

language = "English (US)",

volume = "264",

pages = "13377--13380",

journal = "Journal of Biological Chemistry",

issn = "0021-9258",

publisher = "American Society for Biochemistry and Molecular Biology Inc.",

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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.

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