Isolation and partial characterization of basic fibroblast growth factor from bovine testis.

A basic fibroblast growth factor (FGF) has been purified to homogeneity from bovine testis, using ammonium sulfate precipitation of the crude extract followed by three chromatographic steps, involving cation-exchange, heparin-Sepharose, and reversed-phase HPLC. Gas-phase sequence analysis showed the amino-terminal amino acid sequence of the isolated polypeptide as His-Phe-Lys-Asp-Pro-Lys-Arg-Leu-Tyr-, which is identical to the amino-terminal of the (16-146) fragment of basic FGF previously characterized from corpus luteum, adrenal, and kidney. The purified FGF was shown to have the same biological activity as that of basic FGF (1-146). This finding suggests that basic FGF is present in testis and may act as a local regulator of testicular function. In addition, testicular FGF might play an important role in spermatogenesis and/or the development of testis.