Partial purification of a morphological transforming factor from pig brain.
A protein that changes one type of embryonic rat brain cell in culture from a primitive morphology to one resembling mature glial cell has been purified 400-fold from pig brain. The procedure includes differential centrifugation, ethanol treatment, trypsin digestion and column chromatography with Sephadex G-200 and Sepharose 4B. Although not completely homogeneous, the protein is biologically active at a concentration of 1-10(-8) M. It has a molecular weight of 350 000 and is heat labile. It is inactivated by the extremes of pH and by 8 M urea. The isoionic point is lower than neutrality. The activity is resistant to DNAase, RNAase, periodate and trypsin, but is susceptible to pronase digestion.
D000818:Animals; D001921:Brain / Q000166:cytology* / Q000196:embryology; D001923:Brain Chemistry; D002531:Cerebellum / Q000032:analysis; D004305:Dose-Response Relationship, Drug; D004622:Embryo, Mammalian; D005260:Female; D009419:Nerve Tissue Proteins / Q000302:isolation & purification* / Q000502:physiology; D009457:Neuroglia / Q000502:physiology / Q000648:ultrastructure; D011247:Pregnancy; D051381:Rats; D013552:Swine
D009419:Nerve Tissue Proteins