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Interrelationships between malate-aspartate shuttle and citric acid cycle in rat heart mitochondria
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“Through shared metabolic intermediates and enzymes, the malate–aspartate shuttle and TCA cycle are functionally coupled (115).”
From Regulation and function of the mammalian tricarboxylic acid cycle (2023) · cites this paper as [115]
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WILLIAMSON, J. R., & Corkey, B. E. (1969) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(69)13072-4 · Cited by 867
Self-citationWege des Wasserstoffs in der lebendigen Organisation
Bücher, T., & Klingenberg, M. (1958) · Angewandte Chemie · doi:10.1002/ange.19580701707 · Cited by 616
SYSTEMS USED FOR THE TRANSPORT OF SUBSTRATES INTO MITOCHONDRIA
Chappell, J. (1968) · British Medical Bulletin · doi:10.1093/oxfordjournals.bmb.a070618 · Cited by 453
Adenine Nucleotide Translocation of Mitochondria
Pfaff, E., & Klingenberg, M. (1968) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1968.tb00420.x · Cited by 429
PHOSPHORYLATION COUPLED TO OXIDATION OF DIHYDRODIPHOSPHOPYRIDINE NUCLEOTIDE
Lehninger, A. L. (1951) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)56077-4 · Cited by 421
WILLIAMSON, J. R. (1965) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)97324-2 · Cited by 371
Self-citationThe kinetic properties of citrate synthase from rat liver mitochondria
Shepherd, D., & Garland, P. B. (1969) · Biochemical Journal · doi:10.1042/bj1140597 · Cited by 355
Randle, P. J., ENGLAND, P. J., & Denton, R. M. (1970) · Biochemical Journal · doi:10.1042/bj1170677 · Cited by 274
Pathways of Hydrogen in Mitochondria of Saccharomyces carlsbergensis
von JAGOW, G., & Klingenberg, M. (1970) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1970.tb00890.x · Cited by 241
Inhibitors Tools in Cell Research
Bücher, T., & Sies, H. (1969) · Springer eBooks · doi:10.1007/978-3-642-46158-3 · Cited by 236
Research works printed but not linked: 2
- Williamson, J. R., Jakob, A., and Refino, C.: Carbon and hydrogen shuttles in perfused rat liver. Abs. 8th Int. Cong. Biochem. Switzerland (in press).
- Chance, 1965, Properties and kinetics of reduced pyridine nucleotide fluorescence of the isolated and in vivo rat heart, Biochem. Z., 341, 357
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“Moreover, given that aspartate efflux is dependent upon mitochondrial membrane potential, variability in TCA cycle and ETC function will both influence and be influenced by malate–aspartate shuttle activity (115).”
BackgroundMyocardial utilization of carbohydrate and lipids
Neely, J. R., Rovetto, M. J., & Oram, J. F. (1972) · Progress in Cardiovascular Diseases · doi:10.1016/0033-0620(72)90029-1 · Cited by 509
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“The function of the MAS is antagonized by glutamate oxidation (LaNoue and Williamson, 1971; Du et al., 2013), and there is ample evidence of glutamate oxidation by astrocytes (Hertz et al.”
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Lee, C. F., Chavez, J. D., Garcia‐Menendez, L., Choi, Y. S., Roe, N. D., Chiao, Y. A., Edgar, J. S., Goo, Y. A., Goodlett, D. R., Bruce, J. E., et al. (2016) · Circulation · doi:10.1161/circulationaha.116.022495 · Cited by 342
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Control of maximum rates of glycolysis in rat cardiac muscle.
Kobayashi, K., & Neely, J. R. (1979) · Circulation Research · doi:10.1161/01.res.44.2.166 · Cited by 313
Lai, J. C. K., & Cooper, A. J. L. (1986) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1986.tb00768.x · Cited by 307
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Madiraju, A. K., Qiu, Y., Perry, R. J., Rahimi, Y., Zhang, X., Zhang, D., Camporez, J. P., Cline, G. W., Butrico, G. M., Kemp, B. E., et al. (2018) · Nature Medicine · doi:10.1038/s41591-018-0125-4 · Cited by 306
Significance of skeletal muscle oxidative enzyme enhancement with endurance training.
Gollnick, P. D., & Saltin, B. (1982) · Clinical Physiology · doi:10.1111/j.1475-097x.1982.tb00001.x · Cited by 277
Mitochondrial Transporters as Novel Targets for Intracellular Calcium Signaling
Satrústegui, J., Pardo, B., & del Arco, A. (2007) · Physiological Reviews · doi:10.1152/physrev.00005.2006 · Cited by 261
Borst, P. (2020) · IUBMB Life · doi:10.1002/iub.2367 · Cited by 252
Mick, E., Titov, D. V., Skinner, O. S., Sharma, R., Jourdain, A. A., & Mootha, V. K. (2020) · eLife · doi:10.7554/elife.49178 · Cited by 252
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Panov, A., Orynbayeva, Z., Vavilin, V., & Lyakhovich, V. (2014) · BioMed Research International · doi:10.1155/2014/472459 · Cited by 227
The metabolic significance of anion transport in mitochondria
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Self-citationHong, W., Mo, F., Zhang, Z., Huang, M., & Wei, X. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.00246 · Cited by 182
Yudkoff, M., NELSON, D. S., Daikhin, Y., & Erecińska, M. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)47001-9 · Cited by 169
Mitochondrial GTP regulates glucose-stimulated insulin secretion.
Kibbey, R., Pongratz, R. L., Romanelli, A. J., Wollheim, C., Cline, G., & Shulman, G. (2007) · Cell Metabolism · doi:10.1016/j.cmet.2007.02.008 · Cited by 178
Dienel, G. A., & Cruz, N. F. (2004) · Neurochemistry International · doi:10.1016/j.neuint.2003.10.011 · Cited by 160
LaNoue, K. F., Wałajtys, E. I., & WILLIAMSON, J. R. (1973) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)43375-9 · Cited by 157
Self-citationElectrogenic Characteristics of the Mitochondrial Glutamate-Aspartate Antiporter
LaNoue, K. F., & Tischler, M. E. (1974) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)81269-3 · Cited by 152
Self-citationRegulation of mitochondrial respiration in senescence
Chen, J. C., Warshaw, J. B., & Sanadi, D. R. (1972) · Journal of Cellular Physiology · doi:10.1002/jcp.1040800115 · Cited by 137
Oxidation of cytosolic NADH formed during aerobic metabolism in mammalian cells
Dawson, A. G. (1979) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(79)90417-1 · Cited by 135
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Safer, B., & WILLIAMSON, J. R. (1973) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)44146-x · Cited by 134
Self-citationThe Metabolic Significance of the Malate-Aspartate Cycle in Heart.
Safer, B. (1975) · Circulation Research · doi:10.1161/01.res.37.5.527 · Cited by 128
Smith, C. M., Bryła, J., & WILLIAMSON, J. R. (1974) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)42910-4 · Cited by 128
Self-citationControl of the Removal of Reducing Equivalents from the Cytosol in Perfused Rat Liver
WILLIAMSON, J. R., Jakob, A., & Refino, C. J. (1971) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)45823-7 · Cited by 117
Self-citationCa2+ Activation Kinetics of the Two Aspartate-Glutamate Mitochondrial Carriers, Aralar and Citrin
Contreras, L., Gómez‐Puertas, P., Iijima, M., Kobayashi, K., Saheki, T., & Satrústegui, J. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m610491200 · Cited by 116
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Berkich, D. A., Ola, M. S., Cole, J., Sweatt, A. J., Hutson, S. M., & LaNoue, K. F. (2007) · Journal of Neuroscience Research · doi:10.1002/jnr.21500 · Cited by 114
Self-citationFitzpatrick, S. M., Cooper, A. J. L., & Duffy, T. E. (1983) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1983.tb00835.x · Cited by 113
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LaNoue, K. F., Meijer, A. J., & Brouwer, A. (1974) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(74)90337-3 · Cited by 113
Self-citationExperimental cerebral oligemia and ischemia produced by intracranial hypertension
Marshall, L. F., Durity, F. A., Lounsbury, R., Graham, D. I., Welsh, F. A., & Langfitt, T. W. (1975) · Journal of neurosurgery · doi:10.3171/jns.1975.43.3.0308 · Cited by 109
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Yang, Y. T., & Baldwin, R. L. (1973) · Journal of Dairy Science · doi:10.3168/jds.s0022-0302(73)85178-1 · Cited by 106
Yu, X., White, L. T., Doumen, C., Damico, L. A., LaNoue, K. F., Alpert, N. M., & Lewandowski, E. D. (1995) · Biophysical Journal · doi:10.1016/s0006-3495(95)80080-9 · Cited by 105
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Self-citationCultured retinal neuronal cells and Müller cells both show net production of lactate
Winkler, B. S., Starnes, C. A., Sauer, M. W., Firouzgan, Z., & Chen, S.-C. (2004) · Neurochemistry International · doi:10.1016/j.neuint.2003.08.017 · Cited by 80
Sinasac, D. S., Moriyama, M., Jalil, M. A., Begum, L., Li, M. X., Iijima, M., Horiuchi, M., Robinson, B. H., Kobayashi, K., Saheki, T., et al. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.24.2.527-536.2004 · Cited by 80
Szymczak-Pajor, I., Wenclewska, S., & Śliwińska, A. (2022) · Pharmaceuticals · doi:10.3390/ph15070810 · Cited by 89
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Cederbaum, A. I., Lieber, C. S., Beattie, D. S., & Rubin, E. (1973) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(73)90571-7 · Cited by 78
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Lu, M., Zhou, L., Stanley, W. C., Cabrera, M. E., Saidel, G. M., & Yu, X. (2008) · Journal of Theoretical Biology · doi:10.1016/j.jtbi.2008.05.033 · Cited by 76
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Broeks, M. H., van Karnebeek, C., Wanders, R. J. A., Jans, J. J. M., & Verhoeven‐Duif, N. M. (2021) · Journal of Inherited Metabolic Disease · doi:10.1002/jimd.12402 · Cited by 75
Matthews, P. M., Williams, S. R., Seymour, A.-M., Schwartz, A., Dubé, G. P., Gadian, D. G., & Radda, G. K. (1982) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/0167-4889(82)90008-8 · Cited by 73
Dodd, M. S., Atherton, H. J., Carr, C. A., Stuckey, D. J., West, J. A., Griffin, J. L., Radda, G. K., Clarke, K., Heather, L. C., & Tyler, D. J. (2014) · Circulation Cardiovascular Imaging · doi:10.1161/circimaging.114.001857 · Cited by 69
Schantz, P., SJÖBERG, B., & Svedenhag, J. (1986) · Acta Physiologica Scandinavica · doi:10.1111/j.1748-1716.1986.tb07993.x · Cited by 68
Schäfer, G. (1976) · Biochemical Pharmacology · doi:10.1016/0006-2952(76)90423-8 · Cited by 68
Timmons, J. A., Poucher, S. M., Constantin‐Teodosiu, D., Macdonald, I. A., & Greenhaff, P. L. (1997) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.1997.273.2.e233 · Cited by 68
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Tischler, M. E., Pachence, J. M., WILLIAMSON, J. R., & LaNoue, K. F. (1976) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(76)90282-4 · Cited by 68
Self-citationHofhuis, J., Schueren, F., Nötzel, C., Lingner, T., Gärtner, J., Jahn, O., & Thoms, S. (2016) · Open Biology · doi:10.1098/rsob.160246 · Cited by 59
Regulation of Cardiac Contraction
Ross, J., & Sobel, B. E. (1972) · Annual Review of Physiology · doi:10.1146/annurev.ph.34.030172.000403 · Cited by 62
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Fields, J. H. A. (1983) · Journal of Experimental Zoology · doi:10.1002/jez.1402280306 · Cited by 62
Opie, L. H., & Owen, P. (1975) · Biochemical Journal · doi:10.1042/bj1480403 · Cited by 58
Sato, T., Ohsumi, Y., & Anraku, Y. (1984) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)90891-4 · Cited by 57
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SCHOLZ, T. D., Koppenhafer, S. L., TenEyck, C. J., & Schutte, B. C. (1998) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.1998.274.3.c780 · Cited by 54
Nolte, J., Brdiczka, D. G., & Pette, D. (1972) · Biochimica et Biophysica Acta (BBA) - Enzymology · doi:10.1016/0005-2744(72)90148-9 · Cited by 54
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Zhang, B., Tornmalm, J., Widengren, J., Vakifahmetoglu-Norberg, H., & Norberg, E. (2017) · Journal of Cancer · doi:10.7150/jca.19373 · Cited by 53
Reconstitution of the malate/aspartate shuttle from mitochondria.
Indiveri, C., Krämer, R., & Palmieri, F. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)47685-5 · Cited by 49
Campbell, C., Grapov, D., Fiehn, O., Chandler, C. J., Burnett, D. J., de Souza, E. C. L., Casazza, G. A., Gustafson, M. B., Keim, N. L., Newman, J. W. I., et al. (2014) · PLoS ONE · doi:10.1371/journal.pone.0084260 · Cited by 44
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Beeckmans, S. (1984) · International Journal of Biochemistry · doi:10.1016/0020-711x(84)90131-9 · Cited by 45
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Zhao, J., Tian, M., Zhang, S. J., Delfarah, A., Gao, R., Rao, Y., Savas, A. C., Lu, A., Bubb, L., Lei, X., et al. (2020) · Cell Metabolism · doi:10.1016/j.cmet.2020.04.006 · Cited by 44
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O’Donnell, J. M., Doumen, C., LaNoue, K. F., White, L. T., Yu, X., Alpert, N. M., & Lewandowski, E. D. (1998) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.1998.274.2.h467 · Cited by 44
Self-citationBremer, J., & Davis, E. J. (1975) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/0005-2728(75)90161-9 · Cited by 43
Mitochondrial Transport Processes and Oxidation of NADH by Hypotonically-Treated Boar Spermatozoa
Calvin, J., & Tubbs, P. K. (1978) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1978.tb20929.x · Cited by 43
Dennis, S. C., & Clark, J. B. (1978) · Biochemical Journal · doi:10.1042/bj1720155 · Cited by 43
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Brody, T. (1999) · Elsevier eBooks · doi:10.1016/b978-012134836-6/50007-x · Cited by 43
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Ng, L. E., Vincent, A. S., Halliwell, B. B., & Wong, K. P. (2006) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2006.07.089 · Cited by 41
Substrate anion transport in mitochondria
Brouwer, A., Smits, G., Tas, J., Meijer, A. J., & Tager, J. M. (1973) · Biochimie · doi:10.1016/s0300-9084(73)80025-2 · Cited by 41
Meijer, A. J., & WILLIAMSON, J. R. (1974) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/0005-2728(74)90156-x · Cited by 36
Self-citationMapes, J. P., & Harris, R. A. (1976) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(20)81843-2 · Cited by 35
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Bhattacharya, P. K., Ross, B. D., & Bünger, R. (2009) · Experimental Biology and Medicine · doi:10.3181/0904-mr-135 · Cited by 34
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Mohan, A., Hunt, M. C., Muthukrishnan, S., Barstow, T. J., & Houser, T. A. (2010) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf100714g · Cited by 32
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Davis, E. J., Bremer, J., & Åkerman, K. E. O. (1980) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)85887-8 · Cited by 32
Schroeder, M., Atherton, H. J., Heather, L. C., Griffin, J. L., Clarke, K., Radda, G. K., & Tyler, D. J. (2011) · NMR in Biomedicine · doi:10.1002/nbm.1668 · Cited by 31
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Kakazu, E., Kondo, Y., Kogure, T., Ninomiya, M., Kimura, O. S., Ueno, Y., & Shimosegawa, T. (2013) · Scientific Reports · doi:10.1038/srep03459 · Cited by 30
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Newman, J. J., Strome, D. R., Goodwin, C. W., Mason, A. D., & Pruitt, B. A. (1982) · Metabolism · doi:10.1016/0026-0495(82)90009-9 · Cited by 28
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LaNoue, K. F., & Schoolwerth, A. C. (1984) · New comprehensive biochemistry · doi:10.1016/s0167-7306(08)60318-x · Cited by 27
Self-citationZhang, X., Tomar, N., Kandel, S. M., Audi, S. H., Cowley, A. W., & Dash, R. K. (2021) · Cells · doi:10.3390/cells11010131 · Cited by 26
Junghans, L., Teleki, A., Wijaya, A. W., Becker, M., Schweikert, M., & Takors, R. (2019) · Metabolic Engineering · doi:10.1016/j.ymben.2019.02.005 · Cited by 25
Júnior, A. S. M., Constantin, J., Utsunomiya, K. S., Gilglioni, E. H., Gasparin, F. R. S., Carreño, F. O., de Moraes, S. M. F., Rocha, M., Natali, M. R. M., Ghizoni, C. V. D. C., et al. (2018) · Nutrients · doi:10.3390/nu10111571 · Cited by 22
Orlacchio, A., Campos-Cavieres, M., Pashev, I. G., & Munn, E. A. (1979) · Biochemical Journal · doi:10.1042/bj1770583 · Cited by 22
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Inhibitors of mitochondrial anion transport
Bry⌈a, J. (1980) · Pharmacology & Therapeutics · doi:10.1016/0163-7258(80)90088-1 · Cited by 21
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Aguer, C., Piccolo, B. D., Fiehn, O., Adams, S. H., & Harper, M. (2016) · The FASEB Journal · doi:10.1096/fj.201600914r · Cited by 19
Ylikahri, R., Hassinen, I. E., & Kähönen, M. T. (1971) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(71)80171-7 · Cited by 18
Metadata
- Authors
- LaNoue, K. F., & Williamson, J. R.
- Affiliations
- University of Pennsylvania (US)
- Venue
- Metabolism
- Publisher
- Elsevier BV
- Published
- 1971-02
- Volume
- 20
- Issue
- 2
- Pages
- 119-140
- ISSN
- 0026-0495 (ISSN-L)
- OpenAlex
- W2060829865
- Cited by
- 152
- References
- 36
- Citations by year
- 2026: 2 · 2025: 1 · 2024: 2 · 2023: 1 · 2022: 3 · 2021: 4 · 2020: 8 · 2019: 3 · 2018: 6 · 2017: 2 · 2016: 4 · 2015: 2 · 2014: 4 · 2013: 2
- FWCI
- 5.48
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Metabolism (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Biochemical Acid Research Studies
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
- Keywords
- malate-aspartate shuttle, TCA cycle, heart mitochondria, citrate synthase, oxaloacetate, alpha-ketoglutarate dehydrogenase, ATP/ADP ratio, substrate-level phosphorylation, uncoupled respiration, oligomycin, acetyl-L-carnitine, rat heart
- MeSH terms
- Adenine Nucleotides, Animals, Aspartic Acid, Carnitine, Citric Acid Cycle, Coenzyme A, Fluorometry, Glutamates, Ketoglutaric Acids, Lactates, Malates, Mitochondria, Myocardium, NAD, Oligomycins, Oxaloacetates, Oxidation-Reduction, Oxygen Consumption, Polarography, Rats, In Vitro Techniques
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