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- W2024335843 abstract "1. The tomato fruit contains two alanine 2-oxoglutarate aminotransferase enzymes (EC 2.6.1.2). The minor one can be extracted by Triton X-100. The major enzyme is soluble. No significant changes are observed in the specific activities of these enzymes during tomato ripening. 2. The soluble enzyme has been purified 660-fold by a procedure involving (NH4)2SO4 precipitation, DEAE-cellulose, DEAE-Sephadex and gel filtration on Sephadex G-200. During the purification procedure the enzyme needs protective substances, i.e. glycerol, mercaptoethanol and alanine. The highest specific activity obtained was 120 units/mg of protein. 3. The enzyme reversibly catalyzes the transamination reaction between alanine and 2-oxoglutarate according to the Ping Pong Bi Bi mechanism. The Michaelis constant with respect to alanine is 2.8 mM, to 2-oxoglutarate 0.28 mM, to pyruvate 0.09 mM and to glutamate 2.3 mM." @default.
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- W2024335843 date "1974-06-01" @default.
- W2024335843 modified "2023-10-02" @default.
- W2024335843 title "Partial purification and initial studies of the tomato l-alanine:2-oxoglutarate aminotransferase" @default.
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- W2024335843 doi "https://doi.org/10.1016/0005-2744(74)90513-0" @default.
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