Western blot analysis of porcine corpus luteum heparin binding proteins using antibodies to acidic and basic fibroblast growth factor

Abstract

The 105 000 × g supernatant from homogenates of porcine corpora lutea was chromatographed on a heparin Sepharose affinity column. Bound protein was batch eluted and analyzed on Western blots using antibodies to acidic and basic fibroblast growth factor (FGF). The antibody to acidic FGF reacted specifically with at least four protein bands ranging from 21 to 50 kDa. Three antibodies to human basic FGF (145 residues) generated against either the N-terminal sequence (1–12), the internal sequence (33–43), or the C-terminal end (135–145) also reacted specifically with a total of four different bands. The apparent molecular weights ranged between 20 and 55 kDa. The luteal extract also expresse message for acidic FGF. The results show that there may exist a family of FGF-like molecules in the corpus luteum and demonstrates for the first time the presence of acidic FGF in that tissue.