Gale & Epps (1944) and Gale (1945) observed that the lysine decarboxylase activity of Eseherichia coli '86' was increased by inorganic phosphate (0.1-0-5M), and that the decarboxylation of ornithine by Clo8tridium septiurm was more rapid in phosphate buffers than in citrate buffers of comparable pH. Krebs, Eggleston & Knivett (1955) recently confirmed that the decarboxylation of L-omithine and L-lysine by E8ch. coli was accelerated by the addition of phosphate at pH 6-56-8. The present paper is concerned with a more detailed study of the effects of inorganic and organic phosphates and related substances on the activity of amino acid decarboxylases.
EXPERIMENTAL Material8Buffers. The following buffers were used: phosphate, made froin molar stock solutions ofNa3HPO4 and NaH2PO4; arsenate, made from 0 5M-Na2HAsO4 and N-HCI; citrate made from 0-2M sodium citrate and N-HCI or N-NaOH; tris, made from m aminotrishydroxymethylmethane and N-HCI; acetate, made from sodium acetate and acetic acid; acetate-veronal (Michaelis, 1931), and tris-maleate (Gomori, 1955). A glass electrode and a Pye pH meter were used to measure the pH of these buffers after dilution to the concentrations used in experiments. The additions of enzyme and substrates had little or no effect on the pH.