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- W938656452 abstract "Publisher Summary Glutamate–alanine transaminase is widely distributed. However, its activity in mammalian tissues is somewhat lower than that of glutamic–oxaloacetic transaminase (GOT). In the rat, highest activity is found in the liver with small amounts in skeletal muscle, heart, brain, and very little activity in kidney. The reaction catalyzed by glutamate pyruvate transaminase (GPT) can be assayed in either direction. The reaction can be quantitated in the reverse direction by coupling α-ketoglutarate to the glutamate dehydrogenase reaction and noting the rate of decrease of absorbance at 340 nm of NADH. Appropriate blanks are necessary because pyruvate is a substrate of glutamate dehydrogenase. As for the GOT reaction, pyruvate formation can be measured by the 2, 4-dinitrophenylhydrazone method. The pyruvate-2, 4-dinitrophenylhydrazone can be selectively extracted into toluene. This modification has the advantage that the assay can be carried out with optimum α-ketoglutarate concentrations." @default.
- W938656452 created "2016-06-24" @default.
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- W938656452 date "1985-01-01" @default.
- W938656452 modified "2023-09-27" @default.
- W938656452 title "[12] Glutamate-alanine transaminase" @default.
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- W938656452 doi "https://doi.org/10.1016/s0076-6879(85)13015-6" @default.
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- W938656452 hasPublicationYear "1985" @default.
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