Authors: | Chandrasekhar, S.; Münster, P. N.; Henzel, W. A.; Daud, A. I. |
Article Title: | Purification and characterization of a novel 35-kDa protein from transformed cardiomyocytes |
Abstract: | A 35-kDa protein (designated p35) showing antigenic homology with an N-terminal epitope on the SV-40 large T-antigen oncoprotein was purified from transformed cardiomyocytes. Sequence analysis of several tryptic peptides indicated that p35 was not homologous to previously described sequences. Polyclonal antibody raised against synthetic peptide containing one of the tryptic fragments was used in Western blot analyses to ascertain the tissue-specific pattern of p35 expression. p35 was expressed ubiquitously in adult mouse tissues, and was detected in both embryonic and transformed cardiomyocyte preparations. Subcellular fractionation studies indicated that p35 is an integral membrana protein. Expression of p35 appeared to be regulated by growth conditions as evidenced by a transient decrease in protein levels following the addition of serum to quiescent NIH 3T3 cells. |
Keywords: | controlled study; protein expression; unclassified drug; oncoprotein; sequence analysis; nonhuman; animal cell; mouse; animals; mice; cells, cultured; membrane proteins; animalia; mice, transgenic; cell transformation, neoplastic; gene expression regulation; blotting, western; sequence homology, amino acid; tissue distribution; protein purification; cell transformation; dogs; epitope; membrane protein; immunoblotting; simian virus 40; cell fractionation; sequence homology; databases, factual; virus t antigen; heart muscle cell; cell strain 3t3; myocardium; 3t3 cells; polyacrylamide gel electrophoresis; embryo cell; tissue specificity; peptide mapping; epitopes; t-antigen; antigens, viral, tumor; polyclonal antibody; protein p35; p35; article; cardiomyocytes |
Journal Title: | Cell Biology International |
Volume: | 23 |
Issue: | 4 |
ISSN: | 1065-6995 |
Publisher: | John Wiley & Sons Ltd. |
Date Published: | 1999-04-01 |
Start Page: | 299 |
End Page: | 306 |
Language: | English |
DOI: | 10.1006/cbir.1998.0328 |
PUBMED: | 10600238 |
PROVIDER: | scopus |
DOI/URL: | |
Notes: | Article -- Export Date: 16 August 2016 -- Source: Scopus |