Determination of L-Glutamic Acid by Use of L-Glutamic Acid Decarboxy-lase from Mycobacterium phlei
- 1 March 1956
- journal article
- research article
- Published by Frontiers Media SA in Experimental Biology and Medicine
- Vol. 91 (3) , 370-373
- https://doi.org/10.3181/00379727-91-22266
Abstract
A cell-free preparation from M. phlei with decarboxylase activity towards L-glutamic acid only is described. The preparation is inactive towards 18 other amino acids tested; no glutaminase or glutamoracemase activities were detected. Direct estimation of L-glutamic acid in natural products (containing glutamine) is thus possible. The enzyme may be preserved in solution at 0[degree]C for several months or lyophilized without loss of activity. Optimal decarboxylase activity lies between pH 5.2-5.4, falling off rapidly at pH values of 4 and 6,respectively. Some purification of the enzyme was achieved by fractionation with ammonium sulfate.Keywords
This publication has 7 references indexed in Scilit:
- STUDIES ON l-GLUTAMIC ACID DECARBOXYLASE FROM ESCHERICHIA COLIJournal of Biological Chemistry, 1954
- RÔLES OF GLUTAMINE IN GROWTH OF LACTOBACILLUS ARABINOSUSJournal of Biological Chemistry, 1951
- ENZYMATIC DECARBOXYLATION OF ASPARTIC ACID TO α-ALANINEJournal of Biological Chemistry, 1951
- DETERMINATION OF ASPARTIC AND GLUTAMIC ACIDS BY ENZYMATIC DECARBOXYLATIONJournal of Biological Chemistry, 1951
- Manometric determination of l-aspartic acid in l-asparagineBiochemical Journal, 1950
- Quantitative determination of glutamine and glutamic acidBiochemical Journal, 1948
- Studies on bacterial amino-acid decarboxylasesBiochemical Journal, 1945