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PURIFICATION AND CHARACTERIZATION OF A NOVEL 35-kDa PROTEIN FROM TRANSFORMED CARDIOMYOCYTES

✍ Scribed by Sundararaman Chandrasekhar; Pamela N Münster; William A Henzel; Adil I Daud

Publisher
Elsevier Science
Year
1999
Tongue
English
Weight
640 KB
Volume
23
Category
Article
ISSN
1065-6995

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✦ Synopsis

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 membrane 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.

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