A Growth Factor in Bovine and Human Testes Structurally Related to Basic Fibroblast Growth Factor

作者: Michael T. Story , Joachim Sasse , Daniel Kakuska , Stephen C. Jacobs , Russell K. Lawson

DOI: 10.1016/S0022-5347(17)41649-1

关键词: BiochemistryAmmonium sulfate precipitationAntiserumAmmonium sulfatePeptideGrowth factorIonic strengthBiologyBasic fibroblast growth factorProtease

摘要: Abstract Homogenates of human testes, epididymides and prostate, calf testes are mitogenic for cultured foreskin fibroblasts. The growth factors appear similar in that they inactivated by boiling acid, but not treatment with reducing agent. factor bovine was partially purified from tissue homogenates, prepared high ionic strength buffer (pH 7.6) containing protease inhibitors, ammonium sulfate precipitation two cycles heparin-Sepharose chromatography. also extracted without acidified to pH 4.5, precipitated followed heparin-affinity A predominant 17,500 molecular weight (MW) identified alkaline homogenates its reactivity antisera against synthetic peptides whose sequences corresponded residues 1–12 (amino-terminal), 33–43 (internal) 136–145 (carboxy-terminal) basic fibroblast (bFGF). slightly smaller 16,600 MW peptide acidic extracts reacted the three peptides. 15,500 MW peptide, lacking immunoreactivity antiserum amino-terminal seen. These findings suggest a is present structurally related bFGF. structure appears be altered during isolation procedure.

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