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- W1001480803 abstract "Publisher Summary Branched-chain amino acid transaminase activity is widespread. The supernatant pig heart enzyme is active with at least eleven amino acids but it is most active with the branched-chain amino acids. The activity with various amino acids is in the order: isoleucine > valine > DL-alloisoleucine > leucine. The assay procedures for branched-chain amino acid transaminases involve selective extraction of the branched-chain α-keto acid 2,4-dinitrophenylhydrazone into a suitable organic solvent. In one of the methods used, the reaction mixture contains 20 μmol of L-leucine, 20 μmol of α-ketoglutarate, 200 μmol of Tris (pH 8.6), and enzyme in a final volume of 3.0 ml, 37 ° . After incubation for 10 minutes, the reaction is terminated by the addition of 0.3% 2, 4-dinitrophenylhydrazine in 2 M HCl. The phases are separated by brief centrifugation in a clinical centrifuge. The upper phase is removed and α-ketoisocaproate-2,4-dinitrophenylhydrazone is back extracted into 1.5 ml of 10% w/v sodium carbonate." @default.
- W1001480803 created "2016-06-24" @default.
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- W1001480803 date "1985-01-01" @default.
- W1001480803 modified "2023-09-27" @default.
- W1001480803 title "[13] Glutamate-branched-chain amino acid transaminase" @default.
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- W1001480803 doi "https://doi.org/10.1016/s0076-6879(85)13016-8" @default.
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