Skip to main content
NCBI home page
The Journal of General Physiology logoLink to The Journal of General Physiology
. 1967 Mar 1;50(4):1009–1047. doi: 10.1085/jgp.50.4.1009

Oxidative and Glycolytic Recovery Metabolism in Muscle

Fluorometric observations on their relative contributions

Frans F Jöbsis 1, James C Duffield 1
PMCID: PMC2225690  PMID: 4291915

Abstract

The average degree of reduction of mitochondrial NAD has been measured in the intact toad sartorius by a fluorometric technique. It has been shown that cytoplasmic NADH does not interfere materially with these measurements. The percentage reduction of this respiratory coenzyme has been determined in a number of physiological steady states which are well correlated with fluorometrically determined levels of NADH in suspensions of mitochondria from the hind leg musculature of the toad. In addition, these findings are closely comparable to similar, spectrophotometric measurements on mitochondria from other sources. In the presence of an adequate O2 level a single twitch produces a decrease in fluorescence from the resting steady state which is followed by a slow return to the base line condition. This cycle indicates the intensity and the time course of the oxidative recovery metabolism. The area under this curve is directly related to the number of twitches up to three or four. Greater activity produces a curtailment of oxidative recovery due to glycolysis. In the presence of iodoacetate the linear relation holds for five to seven twitches. At still higher levels of activity a curtailment of the change in NAD level sets in, probably due to the removal of AMP by catabolic reactions.

Full Text

The Full Text of this article is available as a PDF (2.3 MB).

Selected References

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

  1. BETZ A., CHANCE B. INFLUENCE OF INHIBITORS AND TEMPERATURE ON THE OSCILLATION OF REDUCED PYRIDINE NUCLEOTIDES IN YEAST CELLS. Arch Biochem Biophys. 1965 Mar;109:579–584. doi: 10.1016/0003-9861(65)90403-0. [DOI] [PubMed] [Google Scholar]
  2. BETZ A., CHANCE B. PHASE RELATIONSHIP OF GLYCOLYTIC INTERMEDIATES IN YEAST CELLS WITH OSCILLATORY METABOLIC CONTROL. Arch Biochem Biophys. 1965 Mar;109:585–594. doi: 10.1016/0003-9861(65)90404-2. [DOI] [PubMed] [Google Scholar]
  3. CAIN D. F., DAVIES R. E. Breakdown of adenosine triphosphate during a single contraction of working muscle. Biochem Biophys Res Commun. 1962 Aug 7;8:361–366. doi: 10.1016/0006-291x(62)90008-6. [DOI] [PubMed] [Google Scholar]
  4. CARLSON F. D., SIGER A. The mechanochemistry of muscular contraction. I. The isometric twitch. J Gen Physiol. 1960 Sep;44:33–60. doi: 10.1085/jgp.44.1.33. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. CHANCE B., BALTSCHEFFSKY H. Respiratory enzymes in oxidative phosphorylation. VII. Binding of intramitochondrial reduced pyridine nucleotide. J Biol Chem. 1958 Sep;233(3):736–739. [PubMed] [Google Scholar]
  6. CHANCE B., COHEN P., JOBSIS F., SCHOENER B. Intracellular oxidation-reduction states in vivo. Science. 1962 Aug 17;137(3529):499–508. doi: 10.1126/science.137.3529.499. [DOI] [PubMed] [Google Scholar]
  7. CHANCE B., CONNELLY C. M. A method for the estimation of the increase in concentration of adenosine diphosphate in muscle sarcosomes following a contraction. Nature. 1957 Jun 15;179(4572):1235–1237. doi: 10.1038/1791235a0. [DOI] [PubMed] [Google Scholar]
  8. 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]
  9. CHANCE B., WEBER A. THE STEADY STATE OF CYTOCHROME B DURING REST AND AFTER CONTRACTION IN FROG SARTORIUS. J Physiol. 1963 Nov;169:263–277. doi: 10.1113/jphysiol.1963.sp007255. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. CHANCE B., WILLIAMS G. R. Respiratory enzymes in oxidative phosphorylation. I. Kinetics of oxygen utilization. J Biol Chem. 1955 Nov;217(1):383–393. [PubMed] [Google Scholar]
  11. CHANCE B., WILLIAMS G. R. Respiratory enzymes in oxidative phosphorylation. III. The steady state. J Biol Chem. 1955 Nov;217(1):409–427. [PubMed] [Google Scholar]
  12. 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]
  13. DANFORTH W. H., HELMREICH E. REGULATION OF GLYCOLYSIS IN MUSCLE. I. THE CONVERSION OF PHOSPHORYLASE BETA TO PHOSPHORYLASE ALPHA IN FROG SARTORIUS MUSCLE. J Biol Chem. 1964 Oct;239:3133–3138. [PubMed] [Google Scholar]
  14. DUYSENS L. N., AMESZ J. Fluorescence spectrophotometry of reduced phosphopyridine nucleotide in intact cells in the near-ultraviolet and visible region. Biochim Biophys Acta. 1957 Apr;24(1):19–26. doi: 10.1016/0006-3002(57)90141-5. [DOI] [PubMed] [Google Scholar]
  15. ESTABROOK R. W. Fluorometric measurement of reduced pyridine nucleotide in cellular and subcellular particles. Anal Biochem. 1962 Sep;4:231–245. doi: 10.1016/0003-2697(62)90006-4. [DOI] [PubMed] [Google Scholar]
  16. GLOCK G. E., MCLEAN P. The determination of oxidized and reduced diphosphopyridine nucleotide and triphosphopyridine nucleotide in animal tissues. Biochem J. 1955 Nov;61(3):381–388. doi: 10.1042/bj0610381. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Ghosh A., Chance B. Oscillations of glycolytic intermediates in yeast cells. Biochem Biophys Res Commun. 1964 Jun 1;16(2):174–181. doi: 10.1016/0006-291x(64)90357-2. [DOI] [PubMed] [Google Scholar]
  18. HOMMES F. A., SCHUURMANSSTEKHOVEN F. M. APERIODIC CHANGES OF REDUCED NICOTINAMIDE-ADENINE DINUCLEOTIDE DURING ANAEROBIC GLYCOLYSIS IN BREWER'S YEAST. Biochim Biophys Acta. 1964 May 11;86:427–428. doi: 10.1016/0304-4165(64)90081-9. [DOI] [PubMed] [Google Scholar]
  19. Hartree W., Hill A. V. The recovery heat-production in muscle. J Physiol. 1922 Jul 21;56(5):367–381. doi: 10.1113/jphysiol.1922.sp002019. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Hill D. K. The time course of the oxygen consumption of stimulated frog's muscle. J Physiol. 1940 May 14;98(2):207–227. doi: 10.1113/jphysiol.1940.sp003845. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. INFANTE A. A., DAVIES R. E. Adenosine triphosphate breakdown during a single isotonic twitch of frog sartorius muscle. Biochem Biophys Res Commun. 1962 Nov 27;9:410–415. doi: 10.1016/0006-291x(62)90025-6. [DOI] [PubMed] [Google Scholar]
  22. Jöbsis F., Legallais V., O'Connor M. A regulated differential fluorometer for the assay of oxidative metabolism in intact tissues. IEEE Trans Biomed Eng. 1966 Apr;13(2):93–99. doi: 10.1109/tbme.1966.4502412. [DOI] [PubMed] [Google Scholar]
  23. KARPATKIN S., HELMREICH E., CORI C. F. REGULATION OF GLYCOLYSIS IN MUSCLE. II. EFFECT OF STIMULATION AND EPINEPHRINE IN ISOLATED FROG SARTORIUS MUSCLE. J Biol Chem. 1964 Oct;239:3139–3145. [PubMed] [Google Scholar]
  24. SACKTOR B., COCHRAN D. G. DPN-specific alpha-glycerophosphate dehydrogenase in insect flight muscle. Biochim Biophys Acta. 1957 Sep;25(3):649–649. doi: 10.1016/0006-3002(57)90543-7. [DOI] [PubMed] [Google Scholar]
  25. WILLIAMSON J. R. GLYCOLYTIC CONTROL MECHANISMS. I. INHIBITION OF GLYCOLYSIS BY ACETATE AND PYRUVATE IN THE ISOLATED, PERFUSED RAT HEART. J Biol Chem. 1965 Jun;240:2308–2321. [PubMed] [Google Scholar]

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

RESOURCES