title: Purification of bone morphogenetic protein derived from bovine bone matrix.
abstract: Bone morphogenetic protein (BMP) was extracted from the bovine bone matrix and purified by liquid chromatography. The molecular weight of the BMP was 18 kDa by SDS-PAGE, and its pI value was 4.9. Amino acid analysis suggested that the BMP is a polypeptide containing 163 amino acids. In the present study, telopeptide-free type I collagen was used as a carrier of BMP.
authors.affiliation: Department of Oral Surgery, Faculty of Medicine, Mie University, Japan.
authors.forename: K
authors.initials: K
authors.lastname: Bessho
authors.forename: T
authors.initials: T
authors.lastname: Tagawa
authors.forename: M
authors.initials: M
authors.lastname: Murata
mesh_terms: D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001846:Bone Development; D001857:Bone Matrix / Q000032:analysis*; D019485:Bone Morphogenetic Proteins; D002417:Cattle; D002850:Chromatography, Gel; D002853:Chromatography, Liquid; D004591:Electrophoresis, Polyacrylamide Gel; D006133:Growth Substances / Q000302:isolation & purification*; D007525:Isoelectric Focusing; D008297:Male; D008970:Molecular Weight; D009132:Muscles / Q000187:drug effects; D009919:Orchiectomy; D011506:Proteins / Q000302:isolation & purification* / Q000494:pharmacology; D051381:Rats; D011919:Rats, Inbred Strains
chemical_list: D000596:Amino Acids; D019485:Bone Morphogenetic Proteins; D006133:Growth Substances; D011506:Proteins