| First Author | Ueyama H | Year | 1987 |
| Journal | Cell Struct Funct | Volume | 12 |
| Issue | 5 | Pages | 463-70 |
| PubMed ID | 3677181 | Mgi Jnum | J:37727 |
| Mgi Id | MGI:85119 | Doi | 10.1247/csf.12.463 |
| Citation | Ueyama H, et al. (1987) Characterization of acidic actin in mouse sarcoma 180 cells. Cell Struct Funct 12(5):463-70 |
| abstractText | Mouse sarcoma 180 cells have a polypeptide that has the same molecular weight as actin but it is more acidic than alpha-actin. Its tryptic peptide pattern on reversed-phase HPLC was very similar to that of beta + gamma-actin, an actin sample prepared by affinity chromatography on DNase I-Sepharose contained the acidic polypeptide, and monoclonal anti-actin antibody reacted with it; therefore, the polypeptide is considered an actin isoform. The mRNA for this variant actin was identified by analyzing the polypeptides translated in vitro, which indicated that the variant actin is not a post-translationally modified form of any known actin. The variant actin was not stained by polyclonal anti-gizzard actin antibody which reacts with gamma-cytoplasmic, alpha-smooth and gamma-smooth muscle actins, nor by polyclonal anti-skeletal muscle actin antibody which reacts with skeletal, cardiac and alpha-smooth muscle actins. These results suggest that this variant actin is related to beta-cytoplasmic actin or, is a novel species whose N-terminal amino acid sequence is not Glu-Glu-Glu. |
