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Title: Studies in the Enzyme Make-up of Vibrio cholerae: II-Aspartic Acid Deaminase
Authors: Iyer, S N;Dudani, A;Krishna, C R;Shrivastava, D L
subject: Vibrio cholerae;Carbonyl groups;Sulphydryl;Amino
Year: 1954
Description: Aspartic acid deaminase of resting cells of V. cholerae has been studied with partlcular reference to some of its characteristics and the effect of various Inorganic and organic Compounds on its activity. Deamination was most active at pH 8 and was found to be a bimolecular reaction. The initial rate of reaction was uniform, directly proportional to enzyme concentration and dependent On the substrate up to an optimum concentration. The enzyme was not stable in acid pH, particularly below pH 5·0. Activation-Inhibition studies indicated that.the activity of the enzyme was associated with essential metallic radicals, and Sulphydryl,amino and carbonyl groups. .
Standard no: Journal of Scientific and Industrial Research1953,12B,316-24
Appears in Collections:Biochemistry

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