Purification of bovine bone morphogenetic protein by hydroxyapatite chromatography

摘要: Abstract Bovine bone morphogenetic protein (bBMP) induces differentiation of mesenchymal-type cells into cartilage and bone. bBMP has an apparent Mr 18,500 +/- 500 represents less than 0.001% the wet weight tissue. A 34,000 resembling osteonectin is separated by extraction with Triton X-100. 24,000 about half a 22,000 are disassociated from precipitation in 1.5 M guanidine hydrochloride. Aggregates 14,000 insoluble aqueous media; becomes soluble when 6 urea removed solution ultrafiltration. Three separate molecular species Mrs 18,500, 17,500, 17,000 eluted at 0.10, 0.15, 0.20 phosphate ion concentrations, respectively, hydroxy-apatite column. The amino acid composition acidic polylpeptide includes four half-cystine residues; pI 4.9-5.1. component chromoprotein ferritin. NH2-terminal sequence 17,500 simulates histone H2B. may possess calmodulin activity. other proteins induce formation large deposits bone; alone rapidly absorbed small deposits. None formation.