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pubmed:abstractText |
A growth factor was isolated from a neutral pH extract of adult bovine brain. Purification of this polypeptide was achieved by a three step procedure including cationic exchange, heparin-Sepharose affinity and Mono S chromatography. This heparin binding protein had a molecular weight of 18,000 as assessed by silver-stained SDS-PAGE and was not immunologically and structurally related to acidic or basic FGF. Freshly purified protein had a maximal mitogenic effect on bovine brain capillary cells at a concentration of 100 pM. Microsequencing revealed an unique amino-terminal sequence homologous to heparin-binding growth-associated molecule (HB-GAM), a neuronal maturation protein, to pleiotrophin (PTN), a fibroblast cell growth factor and to one form of the putative protein product of the MK gene, a retinoic acid induced-gene.
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