| Literature DB >> 4092056 |
R Lim, J F Miller, D J Hicklin, A A Andresen.
Abstract
Glia maturation factor (GMF) is purified 100 000-fold to apparent homogeneity from bovine brains by a procedure consisting of ammonium sulfate precipitation, column chromatography with diethylaminoethyl-Sephacel, Sephadex G-75, and hydroxylapatite, and a final step using C4 reverse-phase high-performance liquid chromatography. The product shows a single protein band in sodium dodecyl sulfate-polyacrylamide gel. It has a molecular weight of 14 000 and an isoelectric point of pH 5.2. Purified GMF stimulates cultured astroblasts to proliferate and to grow out cell processes with half-maximal activity at 8 ng/mL. A monoclonal antibody raised against partially purified GMF adsorbs the activity of pure GMF and immunologically binds the putative GMF protein band.Entities:
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Year: 1985 PMID： 4092056 DOI： 10.1021/bi00348a035
Source DB: PubMed Journal: Biochemistry ISSN： 0006-2960 Impact factor: 3.162