Skip to main content
NCBI home page
Biochemical Journal logoLink to Biochemical Journal
. 1976 May 1;155(2):297–301. doi: 10.1042/bj1550297

The actin of muscle and fibroblasts.

P J Anderson
PMCID: PMC1172835  PMID: 938480

Abstract

The isolation and quantification of an 18-residue peptide from the N-terminal region of chicken actin was used to quantify the amount of actin in acetone-dried powders of chicken breast muscle and chicken-embryo fibroblasts. Either isotope dilution or double labelling can be used for peptide quantification. About 17% of the protein of chicken breast muscle was estimated to be actin. However, only 0.25% of the protein of chicken-embryo fibroblasts was determined to be actin by quantification of this peptide. The actin content of fibroblasts may be low or the amino acid sequences of muscle and fibroblast actin may differ in the N-terminal region. The methodology used can be extended to examine whether other regions of muscle actin sequence are present in fibroblasts or other cell types.

Full text

PDF
297

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Anderson P. J. Aging effects on the liver aldolase of rabbits. Biochem J. 1974 May;140(2):341–343. doi: 10.1042/bj1400341. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Anderson P. J., Gibbons I., Perham R. N. A comparative study of the structure of muscle fructose 1,6-diphosphate aldolases. Eur J Biochem. 1969 Dec;11(3):503–509. doi: 10.1111/j.1432-1033.1969.tb00802.x. [DOI] [PubMed] [Google Scholar]
  3. Anderson P. J., Randall R. F. Comparison of the subunit and primary structures of the pyruvate kinases from rabbit and sturgeon muscles. Biochem J. 1975 Mar;145(3):575–579. doi: 10.1042/bj1450575. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Bray D., Thomas C. The actin content of fibroblasts. Biochem J. 1975 May;147(2):221–228. doi: 10.1042/bj1470221. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. CARSTEN M. E., KATZ A. M. ACTIN: A COMPARATIVE STUDY. Biochim Biophys Acta. 1964 Sep 4;90:534–541. doi: 10.1016/0304-4165(64)90232-6. [DOI] [PubMed] [Google Scholar]
  6. Collins J. H., Elzinga M. The primary structure of actin from rabbit skeletal muscle. Completion and analysis of the amino acid sequence. J Biol Chem. 1975 Aug 10;250(15):5915–5920. [PubMed] [Google Scholar]
  7. DULBECCO R., VOGT M. One-step growth curve of Western equine encephalomyelitis virus on chicken embryo cells grown in vitro and analysis of virus yields from single cells. J Exp Med. 1954 Feb;99(2):183–199. doi: 10.1084/jem.99.2.183. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Elzinga M., Maron B. J., Adelstein R. S. Human heart and platelet actins are products of different genes. Science. 1976 Jan 9;191(4222):94–95. doi: 10.1126/science.1246600. [DOI] [PubMed] [Google Scholar]
  9. Fishbein W. N. Quantitative densitometry of 1-50 g protein in acrylamide gel slabs with Coomassie blue. Anal Biochem. 1972 Apr;46(2):388–401. doi: 10.1016/0003-2697(72)90312-0. [DOI] [PubMed] [Google Scholar]
  10. Gibbons I., Anderson P. J., Perham R. N. Amino acid sequence homology in the active site of rabbit and sturgeon muscle aldolases. FEBS Lett. 1970 Sep 18;10(1):49–53. doi: 10.1016/0014-5793(70)80413-6. [DOI] [PubMed] [Google Scholar]
  11. Gruenstein E., Rich A., Weihing R. R. Actin associated with membranes from 3T3 mouse fibroblast and HeLa cells. J Cell Biol. 1975 Jan;64(1):223–234. doi: 10.1083/jcb.64.1.223. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. HANSON J., HUXLEY H. E. Quantitative studies on the structure of cross-striated myofibrils. II. Investigations by biochemical techniques. Biochim Biophys Acta. 1957 Feb;23(2):250–260. doi: 10.1016/0006-3002(57)90326-8. [DOI] [PubMed] [Google Scholar]
  13. Hartwig J. H., Stossel T. P. Isolation and properties of actin, myosin, and a new actinbinding protein in rabbit alveolar macrophages. J Biol Chem. 1975 Jul 25;250(14):5696–5705. [PubMed] [Google Scholar]
  14. Pollard T. D., Weihing R. R. Actin and myosin and cell movement. CRC Crit Rev Biochem. 1974 Jan;2(1):1–65. doi: 10.3109/10409237409105443. [DOI] [PubMed] [Google Scholar]
  15. Potter J. D. The content of troponin, tropomyosin, actin, and myosin in rabbit skeletal muscle myofibrils. Arch Biochem Biophys. 1974 Jun;162(2):436–441. doi: 10.1016/0003-9861(74)90202-1. [DOI] [PubMed] [Google Scholar]
  16. Sanger J. W. Presence of actin during chromosomal movement. Proc Natl Acad Sci U S A. 1975 Jun;72(6):2451–2455. doi: 10.1073/pnas.72.6.2451. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Seraydarian K., Briskey E. J., Mommaerts W. F. The modification of actomyosin by alpha- actinin. I. A survey of experimental conditions. Biochim Biophys Acta. 1967 Apr 11;133(3):399–411. doi: 10.1016/0005-2795(67)90544-2. [DOI] [PubMed] [Google Scholar]
  18. Spudich J. A., Watt S. The regulation of rabbit skeletal muscle contraction. I. Biochemical studies of the interaction of the tropomyosin-troponin complex with actin and the proteolytic fragments of myosin. J Biol Chem. 1971 Aug 10;246(15):4866–4871. [PubMed] [Google Scholar]
  19. Tregear R. T., Squire J. M. Myosin content and filament structure in smooth and striated muscle. J Mol Biol. 1973 Jun 25;77(2):279–290. doi: 10.1016/0022-2836(73)90336-7. [DOI] [PubMed] [Google Scholar]
  20. Yang Y. Z., Perdue J. F. Contractile proteins of cultured cells. I. The isolation and characterization of an actin-like protein from cultured chick embryo fibroblasts. J Biol Chem. 1972 Jul 25;247(14):4503–4509. [PubMed] [Google Scholar]

Articles from Biochemical Journal are provided here courtesy of The Biochemical Society

RESOURCES