Abstract
Abstract Enzymic transfer of the amino-group of each of 20 amino-acids to α-oxoglutarate has been studied using lyophilised extracts of rat heart, liver, brain, kidney and skeletal muscle as enzyme source. The glutamate produced was estimated from the carbon dioxide liberated by a bacterial decarboxylase in an autoanalyser. Only asparagine was completely inactive in the transfer. Aminotransferase activity was otherwise unevenly distributed in the tissues. Salicylate (10 mm) was generally inhibitory but it activated the l-tryptophan-α-oxoglutarate aminotransferase.
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