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XB-ART-21585
Biochem Biophys Res Commun 1994 Feb 15;1983:1267-74. doi: 10.1006/bbrc.1994.1179.
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Biologically active BMP-2 in early Xenopus laevis embryos.

Shoda A , Murakami K , Ueno N .


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In this study, we attempted to purify the dimeric BMP-2 from extracts of Xenopus embryos in order to show the presence of BMP-2 activity in the embryos. Immunoreactive BMP-2 protein was found to be a homodimer of an 18 kDa BMP-2 polypeptide linked through disulfide bridge(s). Biological activities of the partially purified dimeric BMP-2 were examined in vitro. The Xenopus BMP-2 induced alkaline phosphatase in a dose-dependent manner in cultured osteoblastic cells, MC3T3-E1. The inducing activity was synergistically enhanced by the presence of retinoic acid. The results showed that the dimeric form of Xenopus BMP-2 has an indistinguishable biological activity from that of mammalian BMP-2.

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Species referenced: Xenopus laevis
Genes referenced: bmp2