Glutamate formation by transamination

More recently, Rowsell (306) has found that glutamate formation by transamination with rat liver and kidney preparations occurs at a faster rate for all L-a-amino acids tested than the rate of aerobic oxidation of these amino acids. In addition, the rates of transamination of L-a-amino acids with a-ketoglutarate were found to be comparable to the rates of ammonia or urea formation in oxidative deamination in slices. The further observations by Rowsell (307) that many L-a-amino acids can transami-nate with pyruvate in rat liver preparations has led to the suggestion that oxidative deamination of some L-a-amino acids may involve initial transamination with pyruvate. It was found that transamination of some L-a-amino acids with pyruvate occurred more rapidly than the aerobic oxidation of the L-amino acids. The resulting alanine formed would then he transaminated with a-ketoglutarate by glutamic-pyruvic transaminase. 

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See also in sourсe #XX -- [ ]

See also in sourсe #XX -- [ ]

See also in sourсe #XX -- [ ]

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