Action of α-methyl-DL-tryptophan in vivo on catabolism of amino acids and their conversion to liver glycogen

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Abstract
AMTP (α-methyl-DL-tryptophan) stimulates the incorporation of (labeled) alanine, glutamate, leucine, isoleucine, histidine, threonine, tryptophan, pyruvate, and acetate into hepatic glycogen. Accompanying this phenomenon is an enhanced rate of oxidation of these substances to carbon dioxide, except for acetate whose oxidation is not influenced by AMTP. AMTP also causes an increased excretion of urea and a rise in body temperature. Presence of the adrenal glands is necessary for the stimulatory action of AMTP on the oxidation of alanine, glutamate, isoleucine, and pyruvate. AMTP-stimulated oxidation of leucine and threonine is only partially dependent upon the adrenal gland. The oxidation of histidine is increased to the same extent by AMTP in both intact and adrenalectomized rats. The ability of AMTP to increase the level of tryptophan pyrrolase activity and, thereby, to create an imbalance of the proportion of amino acids in the rat is implicated in the mechanism responsible for its glyconeogenic property and ability to increase catabolism of amino acids.
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