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• W2007223204 abstract "Actin in transformed sarcoma 180 cells is composed of the nonmuscle β and γ species and of a third, more acidic stable variant termed ζ. Two-dimensional peptide analysis shows that ζ is similar to β actin, differing in the mobility of only one tryptic peptide. Several lines of evidence indicate that ζ is not a modified β-actin species. This third actin species comprises 20% of the total labeled actin, has the same molecular weight as the β and γ actins and has a different mobility in isoelectric focusing gels from that of the known a actins from skeletal, cardiac and vascular smooth muscle. Like β and γ actin, ζ can be extracted with the actin depolymerizing factor from slime mold. Two-dimensional gel electrophoresis (isoelectric focusing) of the 35S-methionine-labeled polypeptides synthesized by a single sarcoma 180 cell showed that all three major actin species coexist within the same cell. This analysis also showed for the first time the coexistence of α and β tubulin, vimentin, α actinin and three other polypeptides present in intermediate-filament-enriched cytoplast cytoskeletons (spots 12, 24 and 31). Determination of the ratio of γ plus β to ζ actin in different cytoskeletal preparations of intact and enucleated sarcoma 180 cells indicated that this actin species is not localized specifically to any of the major actin-containing structures preserved in the cytoskeletons." @default.
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• W2007223204 date "1981-07-01" @default.
• W2007223204 modified "2023-09-23" @default.
• W2007223204 title "Coexistence of three major isoactins in a single sarcoma 180 cell" @default.
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• W2007223204 doi "https://doi.org/10.1016/0092-8674(81)90244-0" @default.
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