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Characterization of Acidic Actin in Mouse Sarcoma 180 Cells

H Ueyama, K Kurokawa, I Sasaki, K Ueda

Cell Struct Funct. 1987 Oct;12(5):463-70.

PMID: 3677181

Abstract:

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.

Chemicals Related in the Paper:

Catalog Number Product Name Structure CAS Number Price
IAR42413882 Monoclonal Anti-Actin, α-Smooth Muscle Monoclonal Anti-Actin, α-Smooth Muscle Price
IAR4248494 Anti-Actin, α-Smooth Muscle antibody, Mouse monoclonal Anti-Actin, α-Smooth Muscle antibody, Mouse monoclonal Price
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