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Biochem J 1993 Apr 15;291 ( Pt 2):413-7.
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Biochemical properties of amphibian bone morphogenetic protein-4 expressed in CHO cells.

Suzuki A , Nishimatsu S , Shoda A , Takebayashi K , Murakami K , Ueno N .

The biochemical properties of recombinant amphibian bone morphogenetic protein-4 (BMP-4), the cDNA of which has been cloned recently by screening of a Xenopus cDNA library, was characterized. The protein was expressed by the transfection of Chinese hamster ovary (CHO) cells with the cDNA cloned into expression vectors bearing a cytomegalovirus promoter or a simian virus 40 promoter. Northern-blot analysis showed that the latter vector was more efficient for Xenopus BMP-4 expression. Specific antiserum against Xenopus BMP-4 peptide demonstrated that the protein is synthesized as a large precursor, processed to the mature form and then secreted from the cells as a homodimer. Analysis of the biological activity in the conditioned medium revealed that Xenopus BMP-4 has a potent alkaline phosphatase-inducing activity on mouse osteoblastic cells.

PubMed ID: 8387268
PMC ID: PMC1132541
Article link: Biochem J

Species referenced: Xenopus laevis
Genes referenced: bmp4

References [+] :
Asashima, Presence of activin (erythroid differentiation factor) in unfertilized eggs and blastulae of Xenopus laevis. 1991, Pubmed, Xenbase