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. 1948;43(2):271–279. doi: 10.1042/bj0430271

Tropomyosin: a new asymmetric protein component of the muscle fibril

K Bailey 1
PMCID: PMC1274679  PMID: 16748400

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Selected References

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

  1. Astbury W. T., Reed R., Spark L. C. An X-ray and electron microscope study of tropomyosin. Biochem J. 1948;43(2):282–287. doi: 10.1042/bj0430282. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Bailey K., Gutfreund H., Ogston A. G. Molecular weight of tropomyosin from rabbit muscle. Biochem J. 1948;43(2):279–281. doi: 10.1042/bj0430279. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Bailey K. Myosin and adenosinetriphosphatase. Biochem J. 1942 Feb;36(1-2):121–139. doi: 10.1042/bj0360121. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Chibnall A. C., Rees M. W., Williams E. F. The total nitrogen content of egg albumin and other proteins. Biochem J. 1943 Sep;37(3):354–359. doi: 10.1042/bj0370354. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Davidson J. N., Waymouth C. Tissue nucleic acids: 1. Ribonucleic acids and nucleotides in embryonic and adult tissue. Biochem J. 1944;38(1):39–50. doi: 10.1042/bj0380039. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Fearon W. R., Foster D. L. The Autolysis of Beef and Mutton. Biochem J. 1922;16(5):564–571. doi: 10.1042/bj0160564. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Foreman F. W. Quantitative Estimation of Aspartic and Glutaminic Acids in the Products of Protein Hydrolysis. Biochem J. 1914 Oct;8(5):463–480. doi: 10.1042/bj0080463. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Gale E. F. Studies on bacterial amino-acid decarboxylases: 5. The use of specific decarboxylase preparations in the estimation of amino-acids and in protein analysis. Biochem J. 1945;39(1):46–52. doi: 10.1042/bj0390046. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Lugg J. W. On the use of mercuric salts and nitrous acid in the colorimetric determination of tyrosine and tryptophan present in solution. Biochem J. 1937 Aug;31(8):1422–1433. doi: 10.1042/bj0311422. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Lugg J. W. Preparation of some protein samples from the fresh leaves of plants and the sulphur distributions of the preparations. Biochem J. 1938 Dec;32(12):2114–2122. doi: 10.1042/bj0322114. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Macpherson H. T. The basic amino-acid content of proteins. Biochem J. 1946;40(4):470–481. [PMC free article] [PubMed] [Google Scholar]
  12. Mirsky A. E., Pauling L. On the Structure of Native, Denatured, and Coagulated Proteins. Proc Natl Acad Sci U S A. 1936 Jul;22(7):439–447. doi: 10.1073/pnas.22.7.439. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Rees M. W. The estimation of threonine and serine in proteins. Biochem J. 1946;40(5-6):632–640. doi: 10.1042/bj0400632. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Sanger F. The free amino groups of insulin. Biochem J. 1945;39(5):507–515. doi: 10.1042/bj0390507. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Tristram G. R. Observations upon the application of partition chromatography to the determination of the monoamino-acids in proteins. Biochem J. 1946;40(5-6):721–733. doi: 10.1042/bj0400721. [DOI] [PMC free article] [PubMed] [Google Scholar]

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