Partial purification of rat and human serum factors inhibiting the G1-S transition in rat hepatocytes.
A low molecular weight compound, which inhibits the G1-S transition in rat hepatocytes, was purified from rat trypsin-treated serum by DEAE-cellulose chromatography and high-performance liquid chromatography on three different stationary phases. This procedure led to a 34500-fold purification with a 29% yield. Inactivation of the purified material by specific enzymes showed that the inhibitor is a glycopeptide containing a peptide moiety, N-acetylneuraminic acid and galactose residues. Amino acid analyses indicated the possible existence of a pentapeptide structure. The same purification procedure was applied to the corresponding human inhibitor. Inactivation by specific enzymes showed that it is also a glycopeptide.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002453:Cell Cycle / Q000187:drug effects; D055598:Chemical Phenomena; D002621:Chemistry; D002851:Chromatography, High Pressure Liquid; D006020:Glycopeptides / Q000302:isolation & purification* / Q000494:pharmacology; D006131:Growth Inhibitors / Q000302:isolation & purification* / Q000494:pharmacology; D006801:Humans; D008099:Liver / Q000166:cytology*; D051381:Rats
D000596:Amino Acids; D006020:Glycopeptides; D006131:Growth Inhibitors