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Purification and Partial Amino Acid Sequence of Osteogenin, a Protein Initiating Bone Differentiation
Open accessAbstract
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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Cited by
Cunningham, N. S., Jenkins, N. A., Gilbert, D. J., Copeland, N. G., Reddi, A. H., & Lee, S.-J. (1995) · Growth Factors · doi:10.3109/08977199509028956 · Cited by 104
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Metadata
- Authors
- Luyten, F. P., Cunningham, N. S., Ma, S., Muthukumaran, N., Hammonds, R. G., Nevins, W. B., Woods, W. I., & Reddi, A. H.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1989-08
- Volume
- 264
- Issue
- 23
- Pages
- 13377-13380
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1517038772
- Cited by
- 409
- References
- 0
- FWCI
- 26.75
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- The paper
- Luyten, F. P., Cunningham, N. S., Ma, S., Muthukumaran, N., Hammonds, R. G., Nevins, W. B., Woods, W. I., & Reddi, A. H. (1989). Purification and Partial Amino Acid Sequence of Osteogenin, a Protein Initiating Bone Differentiation. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(18)80003-5
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