Abstract
Glutamic dehydrogenase (GDH) has not been thought to play an important role in cardiac metabolism in the past. Aspartate aminotransferase was shown to mediate glutamate utilization by mitochondria and there was thought to be little GDH activity in heart mitochondria.1 However, the studies of Godinot et al showed that this enzyme could be purified from pig heart mitochondria and had different properties from the enzyme of beef liver mitochondria.2 Takala et al showed that the perfused rat heart produced ammonia and this appeared to come from GDH rather than the purine nucleotide cycle.3 Ammonia production was stimulated when the perfused heart was working. Studies using pig heart mitochondria indicated that glutamate was oxidized via glutamate dehydrogenase when the mitochondria were oxidizing certain substrates.4 Studies by Nuutinen et al showed that rat heart mitochondria readily formed ammonia from glutamate.5
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© 1986 Plenum Press, New York
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McDaniel, H.G., Jenkins, R.L. (1986). Myocardial Glutamate Dehydrogenase Activity. In: Brautbar, N. (eds) Myocardial and Skeletal Muscle Bioenergetics. Advances in Experimental Medicine and Biology, vol 194. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-5107-8_29
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DOI: https://doi.org/10.1007/978-1-4684-5107-8_29
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