title: The structure and amount of tubulin in cells and tissues.
abstract: The NH2-terminals and amino acid compositions of three carboxymethylcysteine-containing peptides produced from carboxymethylated calf brain tubulin by digestion with elastase have been determined. The 3H/14C ratio obtained when these peptides were generated from mixtures of [14C]carboxymethylated calf brain tubulin and the [3H]carboxymethylated proteins of mouse brain or 3T3 cells and subsequently purified indicated that both mouse brain and 3T3 cells contained protein giving rise to peptides homologous to these peptides. This indicates that the tubulins of calf brain, mouse brain, and 3T3 cells are homologous in the regions of amino acid sequence accounting for the peptides examined. From the 3H/14C ratio of the isolated peptides, 13.5% of the protein of mouse brain and 3.5% of the protein of 3T3 cells were estimated to be tubulin.
mesh_terms: D000818:Animals; D001923:Brain Chemistry; D002250:Carbon Radioisotopes; D002417:Cattle; D002460:Cell Line; D003545:Cysteine / Q000032:analysis; D006023:Glycoproteins / Q000032:analysis; D007461:Iodoacetates; D051379:Mice; D014316:Tritium; D014404:Tubulin / Q000032:analysis
chemical_list: D002250:Carbon Radioisotopes; D006023:Glycoproteins; D007461:Iodoacetates; D014404:Tubulin; D014316:Tritium; D003545:Cysteine