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THE bacterial deaminases of Bact. coli, previously studied, fall into two groups: the first consisting of the deaminases of glycine, dl-alanine and l-(+)glutamic acid, and the second of the deaminases of dl-serine and 1-(-)aspartic acid. In these investigations deaminase activity has been measured in QN (,ug. NH3-N liberated per mg. dry wt. bactdria per hr.). The deaminases of the first group [Stephenson & Gale, 1937] carry out only oxidative deamination and have an activity of the order
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Ernest Frederick Gale (1938) studied this question.
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