Skip to main content
PMC home page
The Journal of General Physiology logoLink to The Journal of General Physiology
. 1963 May 1;46(5):905–928. doi: 10.1085/jgp.46.5.905

Spectrophotometric Studies on Intact Muscle

I. Components of the respiratory chain

Frans F Jöbsis 1
PMCID: PMC2195307  PMID: 14041948

Abstract

The concentrations of the components of the respiratory chain were determined in a variety of intact skeletal muscles by a method of spectrophotometric observation of the transmitted light. In the case of the toad sartorius, these measurements were checked against isolated mitochondrial suspensions prepared from toad skeletal muscles. The relative concentrations of the respiratory components were found to be in reasonable agreement with those of various mitochondrial preparations of mammalian tissues and of the ones from toad skeletal muscle. The rather low cytochrome b and pyridine nucleotide levels in the anoxic minus oxygenated difference spectra were shown to be caused to a certain degree by a partial reduction during the resting steady state. Upon treatment with a strong, reducing agent or after long anoxia some absorption bands appeared with maxima at 591, 562 to 564, and 432 to 434 mµ both in the intact and in the mitochondrial fractions of muscle tissue; they do not appear to be associated with the respiratory chain.

Full Text

The Full Text of this article is available as a PDF (1.3 MB).

Selected References

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

  1. CHANCE B., HESS B. Metabolic control mechanisms. I. Electron transfer in the mammalian cell. J Biol Chem. 1959 Sep;234:2404–2412. [PubMed] [Google Scholar]
  2. CHANCE B., HOLLUNGER G. The interaction of energy and electron transfer reactions in mitochondria. I. General properties and nature of the products of succinate-linked reduction of pyridine nucleotide. J Biol Chem. 1961 May;236:1534–1543. [PubMed] [Google Scholar]
  3. CHANCE B. Spectrophotometry of intracellular respiratory pigments. Science. 1954 Nov 12;120(3124):767–775. doi: 10.1126/science.120.3124.767. [DOI] [PubMed] [Google Scholar]
  4. CHANCE B. The kinetics and inhibition of cytochrome components of the succinic oxidase system. I. Activity determinations and purity criteria. J Biol Chem. 1952 May;197(2):557–565. [PubMed] [Google Scholar]
  5. CHANCE B. The response of mitochondria to muscular contraction. Ann N Y Acad Sci. 1959 Aug 28;81:477–489. doi: 10.1111/j.1749-6632.1959.tb49329.x. [DOI] [PubMed] [Google Scholar]
  6. CHANCE B., WILLIAMS G. R. Respiratory enzymes in oxidative phosphorylation. II. Difference spectra. J Biol Chem. 1955 Nov;217(1):395–407. [PubMed] [Google Scholar]
  7. CHANCE B., WILLIAMS G. R. The respiratory chain and oxidative phosphorylation. Adv Enzymol Relat Subj Biochem. 1956;17:65–134. doi: 10.1002/9780470122624.ch2. [DOI] [PubMed] [Google Scholar]
  8. COLPA-BOONSTRA J. P., MINNAERT K. Myoglobin in heart-muscle preparations and the effect of nitrite treatment. Biochim Biophys Acta. 1959 Jun;33(2):527–534. doi: 10.1016/0006-3002(59)90144-1. [DOI] [PubMed] [Google Scholar]
  9. ESTABROOK R. W. The low temperature spectra of hemoproteins. I. Apparatus and its application to a study of cytochrome c. J Biol Chem. 1956 Dec;223(2):781–794. [PubMed] [Google Scholar]
  10. ESTABROOK R. W. The spectral and enzymatic characterization of cytochrome c1 of liver mitochondria. J Biol Chem. 1958 Feb;230(2):735–750. [PubMed] [Google Scholar]
  11. HILL D. K. Changes in transparency of muscle during a twitch. J Physiol. 1949 May;108(3):292–302. [PubMed] [Google Scholar]
  12. HILL D. K. The effect of stimulation on the diffraction of light by striated muscle. J Physiol. 1953 Mar;119(4):501–512. doi: 10.1113/jphysiol.1953.sp004862. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. HUXLEY A. F., TAYLOR R. E. Local activation of striated muscle fibres. J Physiol. 1958 Dec 30;144(3):426–441. doi: 10.1113/jphysiol.1958.sp006111. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. LERIQUE J., NEKHOROCHEFF J., WAJZER J., WEBER R. Reversible degradation of adenosine triphosphate to inosinic acid during a single muscle twitch. Nature. 1956 Dec 8;178(4545):1287–1288. doi: 10.1038/1781287b0. [DOI] [PubMed] [Google Scholar]
  15. WOOD D. L. Infrared microspectrum of living muscle cells. Science. 1951 Jul 13;114(2950):36–38. doi: 10.1126/science.114.2950.36. [DOI] [PubMed] [Google Scholar]
  16. YONETANI T. Studies on cytochrome oxidase. I. Absolute and difference absorption spectra. J Biol Chem. 1960 Mar;235:845–852. [PubMed] [Google Scholar]

Articles from The Journal of General Physiology are provided here courtesy of The Rockefeller University Press

RESOURCES