Studies in the Enzyme Make-up of Vibrio cholerae: II-Aspartic Acid Deaminase

dc.contributor.author	Iyer, S N
dc.contributor.author	Dudani, A
dc.contributor.author	Krishna, C R
dc.contributor.author	Shrivastava, D L
dc.date.accessioned	2012-07-25T12:03:16Z
dc.date.available	2012-07-25T12:03:16Z
dc.date.issued	1954
dc.identifier.citation	Journal of Scientific and Industrial Research1953,12B,316-24	en
dc.identifier.uri	http://hdl.handle.net/123456789/831
dc.description.abstract	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. .	en
dc.format.extent	940572 bytes
dc.format.mimetype	application/pdf
dc.language.iso	en	en
dc.subject	Vibrio cholerae	en
dc.subject	Carbonyl groups	en
dc.subject	Sulphydryl	en
dc.subject	Amino	en
dc.title	Studies in the Enzyme Make-up of Vibrio cholerae: II-Aspartic Acid Deaminase	en
dc.type	Article	en