Purification and characterization of a neurite extension factor from bovine brain.
作者： D. Kligman , D. R. Marshak
关键词:
摘要: The extension of neurites by chicken embryo cerebral cortical neurons can be measured quantitatively at low cell density in serum-free, defined medium. An acidic, heat-stable protein fraction from bovine brain has been shown to have neurite activity this assay. We report the use reversed-phase HPLC purify a factor apparent homogeneity. was characterized NaDodSO4/PAGE. In presence reducing agents, migrated as single band, with an molecular weight 6500. absence showed bands weights 6500, 21,000-22,000, 30,000, and 40,000. Reduction S-carboxymethylation abolished all biological resulted shift 11,000. amino acid composition purified neurite-extension nearly identical that S100 beta. sequences peptides derived trypsin or cyanogen bromide digests were those found beta accounted for 71 91 acids protein. However, three obtained digestion nonreduced appeared disulfide-linked dimers. Our results indicate activity, extension, which is critical development nervous system, associated disulfide form
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