Purification of bone morphogenetic protein derived from bovine bone matrix.
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.
Bessho
K
K
Department of Oral Surgery, Faculty of Medicine, Mie University, Japan.
Tagawa
T
T
Murata
M
M
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
D000596:Amino Acids; D019485:Bone Morphogenetic Proteins; D006133:Growth Substances; D011506:Proteins