Procedures to rapidly isolate fibroblast growth factor (FGF)-like activity from a number of tissue sources (lung, plasma, brain, ovary, corpus luteum, pituitary, chondrosarcoma) of bovine, porcine or rat origin are described. In addition, immunoblotting experiments using well characterized and specific rabbit polyclonal anti-fibroblast growth factor β (anti-FGF-β) sera have been performed. Besides documenting the first report of the isolation of FGF-β from bovine lung and plasma, these studies provide evidence for the existence of higher-molecular-mass proteins with FGF-β-like immunoreactivity. For example, in addition to new truncated forms of the acidic and basic FGF (FGF-α and FGF-β), respectively, other higher-molecular-mass immunoreactive proteins were detected in bovine, pig and rat brain, and in rat chondrosarcoma. The tissue distribution of these immunoreactive proteins and their competitive inhibition characteristics mitigate against the possibility that the polyclonal antisera are cross-reacting non-specifically with common cellular proteins. Rather, the data suggest that the immunoblotting technique is either detecting other proteins structurally related to FGF-β or alternatively FGF-β is strongly bound to specific carrier proteins (e.g. heparan sulphate proteoglycan fragments) associated with their transport and recognition at the cellular level. © 1989.
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