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. 1967 Oct;105(1):361–370. doi: 10.1042/bj1050361

3-Methylhistidine in actin and other muscle proteins

P Johnson 1, C I Harris 1, S V Perry 1
PMCID: PMC1198308  PMID: 6056634

Abstract

1. By the use of the extended elution system for basic amino acid analysis, 3-methylhistidine has been detected in hydrolysates of actin isolated from mammalian, fish and bird skeletal muscle. 2. Evidence is presented to indicate that 3-methylhistidine forms part of the primary structure and that in rabbit actin this residue is restricted to one peptide fraction obtained from the tryptic digest. 3. Rabbit skeletal-muscle actin has a 3-methylhistidine:histidine ratio 1:7·6, indicating a minimum molecular weight of 47600. 4. Adult rabbit myosin contains approximately 2 3-methylhistidine residues/mol. These residues are localized in the heavy meromyosin part of the molecule, and are restricted to the major component obtained after succinylation.

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Selected References

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

  1. AMBLER R. P., REES M. W. Epsilon-N-Methyl-lysine in bacterial flagellar protein. Nature. 1959 Jul 4;184:56–57. doi: 10.1038/184056b0. [DOI] [PubMed] [Google Scholar]
  2. Asatoor A. M., Armstrong M. D. 3-methylhistidine, a component of actin. Biochem Biophys Res Commun. 1967 Jan 23;26(2):168–174. doi: 10.1016/0006-291x(67)90229-x. [DOI] [PubMed] [Google Scholar]
  3. BAGLIONI C. An improved method for the fingerprinting of human hemoglobin. Biochim Biophys Acta. 1961 Apr 1;48:392–396. doi: 10.1016/0006-3002(61)90490-5. [DOI] [PubMed] [Google Scholar]
  4. BAILEY K. End-group assay in some proteins of the keratin-myosin group. Biochem J. 1951 Jun;49(1):23–27. doi: 10.1042/bj0490023. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Bailey K. Tropomyosin: a new asymmetric protein component of the muscle fibril. Biochem J. 1948;43(2):271–279. doi: 10.1042/bj0430271. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. CARSTEN M. E., MOMMAERTS W. F. A study of actin by means of starch gel electrophoresis. Biochemistry. 1963 Jan-Feb;2:28–32. doi: 10.1021/bi00901a006. [DOI] [PubMed] [Google Scholar]
  7. COCKS D. H., DENNIS P. O., NELSON T. H. ISOLATION OF 3-METHYL HISTIDINE FROM WHALEMEAT EXTRACT AND THE PREPARATION OF SOME DERIVATIVES. Nature. 1964 Apr 11;202:184–185. doi: 10.1038/202184a0. [DOI] [PubMed] [Google Scholar]
  8. CRESTFIELD A. M., MOORE S., STEIN W. H. The preparation and enzymatic hydrolysis of reduced and S-carboxymethylated proteins. J Biol Chem. 1963 Feb;238:622–627. [PubMed] [Google Scholar]
  9. Dent C. E. A study of the behaviour of some sixty amino-acids and other ninhydrin-reacting substances on phenol-;collidine' filter-paper chromatograms, with notes as to the occurrence of some of them in biological fluids. Biochem J. 1948;43(2):169–180. [PMC free article] [PubMed] [Google Scholar]
  10. HIRS C. H., MOORE S., STEIN W. H. Peptides obtained by tryptic hydrolysis of performic acid-oxidized ribonuclease. J Biol Chem. 1956 Apr;219(2):623–642. [PubMed] [Google Scholar]
  11. Johnson P., Harris C. I., Perry S. V. 3-methylhistidine in actin and other muscle proteins. Biochem J. 1967 Jun;103(3):79P–79P. [PMC free article] [PubMed] [Google Scholar]
  12. Jones J. M., Perry S. V. The biological activity of subfragment 1 prepared from heavy meromyosin. Biochem J. 1966 Jul;100(1):120–129. doi: 10.1042/bj1000120. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. KASAI M., NAKANO E., OOSAWA F. POLYMERIZATION OF ACTIN FREE FROM NUCLEOTIDES AND DIVALENT CATIONS. Biochim Biophys Acta. 1965 Mar 29;94:494–503. doi: 10.1016/0926-6585(65)90058-0. [DOI] [PubMed] [Google Scholar]
  14. KRANS H. M., VAN EIJKH, WESTENBRINK H. G. A STUDY OF G-ACTIN. Biochim Biophys Acta. 1965 Apr 12;100:193–201. doi: 10.1016/0304-4165(65)90441-1. [DOI] [PubMed] [Google Scholar]
  15. KUBY S. A., NODA L., LARDY H. A. Adenosinetriphosphate-creatine transphosphorylase. I. Isolation of the crystalline enzyme from rabbit muscle. J Biol Chem. 1954 Jul;209(1):191–201. [PubMed] [Google Scholar]
  16. LAKI K., MARUYAMA K., KOMINZ D. R. Evidence for the interaction between tropomyosin and actin. Arch Biochem Biophys. 1962 Aug;98:323–330. doi: 10.1016/0003-9861(62)90190-x. [DOI] [PubMed] [Google Scholar]
  17. LOWEY S., COHEN C. Studies on the structure of myosin. J Mol Biol. 1962 Apr;4:293–308. doi: 10.1016/s0022-2836(62)80007-2. [DOI] [PubMed] [Google Scholar]
  18. MARTONOSI A., GOUVEA M. A., GERGELY J. Studies on actin. IV. Actin as a component of myosin-B. J Biol Chem. 1960 Nov;235:3169–3173. [PubMed] [Google Scholar]
  19. MIHASHI K. MOLECULAR CHARACTERISTICS OF G-ADP ACTIN. Arch Biochem Biophys. 1964 Sep;107:441–448. doi: 10.1016/0003-9861(64)90300-5. [DOI] [PubMed] [Google Scholar]
  20. MUELLER H. MOLECULAR WEIGHT OF MYOSIN AND MEROMYOSINS BY ARCHIBALD EXPERIMENTS PERFORMED WITH INCREASING SPEED OF ROTATIONS. J Biol Chem. 1964 Mar;239:797–804. [PubMed] [Google Scholar]
  21. Mueller H. Characterization of the molecular region containing the active sites of myosin. J Biol Chem. 1965 Oct;240(10):3816–3828. [PubMed] [Google Scholar]
  22. Oppenheimer H., Bárány K., Hamoir G., Fenton J. Polydispersity of succinylated myosin. Arch Biochem Biophys. 1966 Jul;115(1):233–234. doi: 10.1016/s0003-9861(66)81064-0. [DOI] [PubMed] [Google Scholar]
  23. PERRY S. V., CORSI A. Extraction of proteins other than myosin from the isolated rabbit myofibril. Biochem J. 1958 Jan;68(1):5–12. doi: 10.1042/bj0680005. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. PERRY S. V. The chromatography of L-myosin on diethylaminoethylcellulose. Biochem J. 1960 Jan;74:94–101. doi: 10.1042/bj0740094. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. PERRY S. V., ZYDOWO M. The nature of the extra protein fraction from myofibrils of striated muscle. Biochem J. 1959 Feb;71(2):220–228. doi: 10.1042/bj0710220. [DOI] [PMC free article] [PubMed] [Google Scholar]
  26. RAFTERY M. A., COLE R. D. Tryptic cleavage at cysteinyl peptide bonds. Biochem Biophys Res Commun. 1963 Mar 25;10:467–472. doi: 10.1016/0006-291x(63)90381-4. [DOI] [PubMed] [Google Scholar]
  27. RYLE A. P., SANGER F., SMITH L. F., KITAI R. The disulphide bonds of insulin. Biochem J. 1955 Aug;60(4):541–556. doi: 10.1042/bj0600541. [DOI] [PMC free article] [PubMed] [Google Scholar]
  28. SEARLE J. M., WESTALL R. G. The occurrence of free methylhistidine in urine. Biochem J. 1951 Apr;48(4):1–1. [PubMed] [Google Scholar]
  29. SJOQUIST J. Determination of amino acids as phenyl thiohydantoin derivatives. III. Quantitative determination of 3-phenyl-2-thiohydantoins from paper chromatograms. Biochim Biophys Acta. 1960 Jun 17;41:20–30. doi: 10.1016/0006-3002(60)90364-4. [DOI] [PubMed] [Google Scholar]
  30. TALLAN H. H., STEIN W. H., MOORE S. 3-Methylhistidine, a new amino acid from human urine. J Biol Chem. 1954 Feb;206(2):825–834. [PubMed] [Google Scholar]
  31. WITTMANN H. G., BRAUNITZER G. Isolation and composition of all tryptic peptides of TMV. Virology. 1959 Dec;9:726–728. doi: 10.1016/0042-6822(59)90170-9. [DOI] [PubMed] [Google Scholar]

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