Premium
High yield isolation of BMP‐2 from bone and in vivo activity of a combination of BMP‐2/TGF‐β 1
Author(s) -
Sibiya Sibusiso J.,
Olivier Eugene I.,
Duneas Nicolaas
Publication year - 2013
Publication title -
journal of biomedical materials research part a
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.849
H-Index - 150
eISSN - 1552-4965
pISSN - 1549-3296
DOI - 10.1002/jbm.a.34365
Subject(s) - in vivo , bone morphogenetic protein , matrix (chemical analysis) , materials science , bone morphogenetic protein 2 , transforming growth factor , yield (engineering) , biological activity , chromatography , biophysics , in vitro , microbiology and biotechnology , biology , biochemistry , chemistry , metallurgy , gene
A high‐yield purification procedure for protein fractions derived from porcine bone matrix extracts is described, which has a high abundance of bone morphogenetic protein‐2 (BMP‐2). Naturally derived pBMP‐2, ∼5 μg per kilogram of porcine bone matrix, was isolated by using a 300 kDa membrane before chromatographic processing on heparin affinity media. The elution of pBMP‐2 and transforming growth factor‐β 1 (TGF‐β 1 ) revealed morphogen peaks that were unresolved on Prosep ® medium, but resolved on hydroxyapatite medium. Antagonism was observed in animal studies when the two proteins were combined in specific doses. The TGF‐β 1 fraction alone was not active in the rodent heterotopic in vivo bioassay, confirming previously obtained results. © 2012 Wiley Periodicals, Inc. J Biomed Mater Res Part A: 101A: 641–646, 2013.