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Journal of Neuroscience, Vol 4, 75-83, Copyright © 1984 by Society for Neuroscience
Identification and purification of glial growth factor
GE Lemke and JP Brockes
Cultured rat Schwann cells are stimulated to divide by a protein growth
factor, present in extracts of bovine brain and pituitary, which we have
named glial growth factor (GGF). Two lines of evidence indicate that GGF
activity in both brain and pituitary resides in a protein of Mr = 31,000.
(1) Four independently isolated monoclonal antibodies that
immunoprecipitate the activity react with an antigen of this molecular
weight in sodium dodecyl sulfate (SDS)-polyacrylamide gels. (2) After
SDS-polyacrylamide gel electrophoresis of partially purified preparations,
mitogenic activity on Schwann cells is recovered at this molecular weight.
GGF has been purified approximately 10(5)-fold to apparent homogeneity from
bovine pituitary anterior lobes by a combination of column chromatography
steps and preparative SDS gel electrophoresis. Purified human
platelet-derived growth factor, a molecule with properties similar to those
of GGF, is inactive on Schwann cells and therefore appears to be distinct.
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