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. 1971 Feb 1;48(2):340–347. doi: 10.1083/jcb.48.2.340

THE M BAND

Studies with Fluorescent Antibody Staining

Ellen Kundrat 1, Frank A Pepe 1
PMCID: PMC2108176  PMID: 4101522

Abstract

The M band can be extracted from fibrils suspended in 5 mM Tris buffer, pH 8.0, for 15 min. The M band is completely removed only from fibrils of sarcomere lengths greater than 2.1 µ. Extraction does not alter the fluorescent antimyosin staining pattern of the A band, thus providing strong evidence that no alteration of the structural integrity of the thick filament has occurred. Fluorescent antibody staining of the M band of unextracted fibrils can be prevented specifically by absorbing the fluorescent antibody with extracted M band material prior to staining. This verifies the specificity of the extraction procedure.

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Selected References

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

  1. Corsi A., Muscatello U., Ronchetti I. Electron microscope observations of the location of actin and tropomyosin in the rabbit myofibril. J Ultrastruct Res. 1967 Aug;19(3):260–272. doi: 10.1016/s0022-5320(67)80220-x. [DOI] [PubMed] [Google Scholar]
  2. Elliott G. F., Lowy J., Millman B. M. X-ray diffraction from living striated muscle during contraction. Nature. 1965 Jun 26;206(991):1357–1358. doi: 10.1038/2061357a0. [DOI] [PubMed] [Google Scholar]
  3. Masaki T., Takaiti O., Ebashi S. "M-substance", a new protein constituting the M-line of myofibrils. J Biochem. 1968 Dec;64(6):909–910. doi: 10.1093/oxfordjournals.jbchem.a128975. [DOI] [PubMed] [Google Scholar]
  4. 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]
  5. Pepe F. A. Analysis of antibody staining patterns obtained with striated myofibrils in fluorescence microscopy and electron microscopy. Int Rev Cytol. 1968;24:193–231. doi: 10.1016/s0074-7696(08)61400-x. [DOI] [PubMed] [Google Scholar]
  6. Pepe F. A. Some aspects of the structural organization of the myofibril as revealed by antibody--staining methods. J Cell Biol. 1966 Mar;28(3):505–525. doi: 10.1083/jcb.28.3.505. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Pepe F. A. The myosin filament. I. Structural organization from antibody staining observed in electron microscopy. J Mol Biol. 1967 Jul 28;27(2):203–225. doi: 10.1016/0022-2836(67)90016-2. [DOI] [PubMed] [Google Scholar]
  8. Pepe F. A. The myosin filament. II. Interaction between myosin and actin filaments observed using antibody staining in fluorescent and electron microscopy. J Mol Biol. 1967 Jul 28;27(2):227–236. doi: 10.1016/0022-2836(67)90017-4. [DOI] [PubMed] [Google Scholar]
  9. Stromer M. H., Hartshorne D. J., Mueller H., Rice R. V. The effect of various protein fractions on Z- and M-line reconstitution. J Cell Biol. 1969 Jan;40(1):167–178. doi: 10.1083/jcb.40.1.167. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. TUNIK B., HOLTZER H. The distribution of muscle antigens in contracted myofibrils determined by fluorescein-labeled antibodies. J Biophys Biochem Cytol. 1961 Oct;11:67–75. doi: 10.1083/jcb.11.1.67. [DOI] [PMC free article] [PubMed] [Google Scholar]

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