Abstract
We describe two subpopulations of actin antibodies isolated by affinity chromatography from a polyclonal antibody to chicken gizzard actin. One subpopulation recognizes γ actins from smooth muscle and nonmuscle cells, but does not recognize α actin from skeletal muscle. The other subpopulation recognizes determinants that are common to a actin from skeletal muscle and the two γ actin isotypes. Neither antibody recognizes cytoplasmic β actin. Both antibodies recognize only actins or molecules with determinants that are also present in actins. By immunofluorescence we found that the anti-γ actin colocalizes with mitochondria in fibers of mouse diaphragm, and that it does not bind detectably to the I bands of sarcomeres. The antibody that recognizes both α and γ actins stains I bands intensely, as expected. We interpret these observations as preliminary evidence for selective association of γ actin with skeletal muscle mitochondria and, more broadly, as evidence for subcellular sorting of isoactins.
Original language | English (US) |
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Pages (from-to) | 1093-1103 |
Number of pages | 11 |
Journal | Cell |
Volume | 32 |
Issue number | 4 |
DOIs | |
State | Published - Apr 1983 |
Externally published | Yes |
ASJC Scopus subject areas
- Biochemistry, Genetics and Molecular Biology(all)