Presence of high molecular weight forms of BMP-2 in early Xenopus embryos.
Using polyclonal antibodies which recognize 18 kDa BMP-2, we have previously demonstrated that the major BMP-2 protein in Xenopus embryo extracts is monomeric and not dimerized whereas, the mammalian counterpart derived from bone extract was purified as a dimeric protein. In this study, the same antibodies (Ab383) were used to detect high molecular weight forms of Xenopus BMP-2. Partial purification of the immunoreactive 18 kDa BMP-2 from Xenopus embryo extract by gel filtration, heparin-Sepharose affinity chromatography and preparative SDS-PAGE resulted in co-purification and identification of higher molecular forms of BMP-2 of 110 kDa and 36 kDa. Diagonal SDS-PAGE analysis suggested that they are homodimer and multimer of the 18 kDa species, respectively, linked through disulfide bridge(s).
Shoda
A
A
Institute of Applied Biochemistry, University of Tsukuba, Ibaraki, Japan.
Murakami
K
K
Ueno
N
N
D000818:Animals; D019485:Bone Morphogenetic Proteins; D004625:Embryo, Nonmammalian / Q000378:metabolism; D006133:Growth Substances / Q000737:chemistry / Q000276:immunology / Q000378:metabolism*; D007120:Immunochemistry; D008958:Models, Molecular; D008970:Molecular Weight; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry / Q000276:immunology / Q000378:metabolism*; D014982:Xenopus laevis / Q000378:metabolism*
D019485:Bone Morphogenetic Proteins; D006133:Growth Substances; D011506:Proteins