ISOLATION AND CHARACTERIZATION OF 2 DIFFERENT MOLECULAR-FORMS OF BASIC FIBROBLAST GROWTH-FACTOR EXTRACTED FROM HUMAN PLACENTAL TISSUE

Basic fibroblast growth factor (bFGF) was purified to homogeneity from human placental tissue on a semi-large scale. Placental bFGF consists of two proteins of apparent molecular masses 16 000 and 18 000 dalton, as determined by sodium dodecyl sulphate polyacrylamide gel electrophoresis under non-reducing conditions. Microsequence analysis showed that both proteins have the same N-terminal sequence Pro-Ala-Leu-Pro-Glu-Asp-Gly-Gly-Ser-Gly-Ala-Phe..., which is identical with that of (1-146) bFGF extracted from human brain. After reduction by dithiothreitol or mercaptoethanol, placental bFGF appears as a single protein of 16 000 dalton. The reduced protein displays the same ability to stimulate the proliferation of CCL39 fibroblasts as the non-reduced doublet. These data indicate that bFGF extracted from placental tissue consists of two proteins with different apparent molecular masses which do not differ in their N-terminal sequence but in their oxidation state.