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Prostatic growth factor: purification and structural relationship to basic fibroblast growth factor.

M T Story·J Sasse·S C Jacobs·R K Lawson
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Abstract

Prostatic growth factor (PrGF) was purified from alkaline homogenates of human benign prostatic hyperplastic tissue by a combination of ammonium sulfate precipitation, heparin affinity chromatography, and cation-exchange chromatography. The 17,600-dalton, basic (pI 10.2) PrGF is related to basic fibroblast growth factor (bFGF) since antisera raised against synthetic peptides with sequence homologies corresponding to an internal peptide and amino- and carboxyl-terminal peptides of bFGF react with the growth factor. The growth factor appears larger than bFGF, suggesting that additional amino-terminal sequences may be present as a result of alkaline extraction in the presence of protease inhibitors.

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Amino Acid SequenceAmmonium SulfateChromatography, AffinityChromatography, Ion ExchangeCollodionElectrophoresis, Polyacrylamide GelFibroblast Growth FactorsHumansHyperplasiaImmunoenzyme TechniquesMaleMolecular WeightProstateTissue ExtractsJournal ArticleResearch Support, U.S. Gov't, P.H.S.

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M T Story, J Sasse, S C Jacobs, R K Lawson. 1987-06-30. Prostatic growth factor: purification and structural relationship to basic fibroblast growth factor.. https://doi.org/10.1021/bi00387a016

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