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Identification and quantification of actin isoforms in vertebrate cells and tissues
Author(s) -
Otey C. A.,
Kalnoski M. H.,
Bulinski J. C.
Publication year - 1987
Publication title -
journal of cellular biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.028
H-Index - 165
eISSN - 1097-4644
pISSN - 0730-2312
DOI - 10.1002/jcb.240340205
Subject(s) - gene isoform , actin , cytoskeleton , biology , homology (biology) , microbiology and biotechnology , spleen , vertebrate , biochemistry , amino acid , gene , immunology , cell
The cytoskeletal protein actin exists in vertebrates as six different isoforms, which are difficult to identify conclusively because of a high degree (>90%) of overall sequence homology. We have used IEF immunoblotting in combination with a panel of isoform‐specific and ‐selective antibodies to analyze the actin isoform composition of nine tissues from adult rat. In three nonmuscle tissues (lung, spleen, and testis), we detected a previously unreported isoform that we identified as smooth muscle α. The IEF immunoblot technique was also used to quantify the proportions of the isoforms expressed in these nine rat tissues.

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