TY - JOUR
T1 - Identification and characterization of multiple forms of actin
AU - Garrels, James I.
AU - Gibson, Wade
N1 - Funding Information:
We are grateful to Drs . David Schubert and Tony Hunter for suggestions and helpful discussions during the course of this work . We thank Drs . E . P . Geiduschek and Bart Sefton for criticism of the manuscript, and Ms . Bonnie Harkins for her help in its preparation . This work was supported by grants from the NIH and the Muscular Dystrophy Association to Dr . David Schubert and by a grant from the National Cancer Institute to Dr. Walter Eckhart . J.I .G. is a predoctoral fellow at the University of California, San Diego, and is supported by a training grant from the NIH . W.G . was a postdoctoral fellow of the NIH .
PY - 1976/12
Y1 - 1976/12
N2 - Multiple forms of actin have been found in a variety of mammalian cell lines and tissues by the use of high resolution, two-dimensional gel electrophoresis. One form (α actin) was found only in differentiated muscle cells, and its synthesis is induced during myogenesis in culture. Two other forms (β and γ actin) are present in all nonmuscle cell types examined, and they continue to be synthesized in cultured muscle cells after fusion. Tryptic peptide comparisons have shown that muscle actin is distinguished from the two "nonmuscle" actins by several peptide differences, and that the two nonmuscle actins are nearly identical. All three forms contain equimolar amounts of Nτ-methylhistidine, and extensive controls have shown no evidence of artifactual heterogeneity. In addition to the three major actins, two other proteins were identified as probable forms of actin by affinity for DNAase I-agarose. These proteins are similar in charge and molecular weight to the major actin forms, but are unstable and have lifetimes in the cell of <2 hr.
AB - Multiple forms of actin have been found in a variety of mammalian cell lines and tissues by the use of high resolution, two-dimensional gel electrophoresis. One form (α actin) was found only in differentiated muscle cells, and its synthesis is induced during myogenesis in culture. Two other forms (β and γ actin) are present in all nonmuscle cell types examined, and they continue to be synthesized in cultured muscle cells after fusion. Tryptic peptide comparisons have shown that muscle actin is distinguished from the two "nonmuscle" actins by several peptide differences, and that the two nonmuscle actins are nearly identical. All three forms contain equimolar amounts of Nτ-methylhistidine, and extensive controls have shown no evidence of artifactual heterogeneity. In addition to the three major actins, two other proteins were identified as probable forms of actin by affinity for DNAase I-agarose. These proteins are similar in charge and molecular weight to the major actin forms, but are unstable and have lifetimes in the cell of <2 hr.
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U2 - 10.1016/0092-8674(76)90142-2
DO - 10.1016/0092-8674(76)90142-2
M3 - Article
C2 - 1017015
AN - SCOPUS:0017272548
SN - 0092-8674
VL - 9
SP - 793
EP - 805
JO - Cell
JF - Cell
IS - 4 PART 2
ER -