Record Details


Field	Value

Title	Purification of L-asparaginase from a bacteria Erwinia carotovora and effect of a dihydropyrimidine derivative on some of its kinetic parameters

Creator	Kamble, V P Rao, R Srinivasa Borkar, Prita S

Subject	Erwinia carotovora L-Asparaginase activity Dihydropyrimidine derivative

Description	391-394 L-Asparaginase shows antileukemic activity and is generally administered in the body in combination with other anticancer drugs like pyrimidine derivatives. In the present study, L-asparaginase was purified from a bacteria Erwinia carotovora and the effect of a dihydropyrimidine derivative (1-amino-6-methyl-4-phenyl-2-thioxo, 1,2,3,4-tetrahydropyrimidine-5-carboxylic acid methyl ester) was studied on the kinetic parameters Km and Vmax of the enzyme using L-asparagine as substrate. The enzyme had optimum activity at pH 8.6 and temperature 35°C, both in the absence and presence of pyrimidine derivative and substrate saturation concentration at 6 mg/ml. For the enzymatic reaction in the absence and presence (1 to 3 mg/ml) of dihydropyrimidine derivative, Km values were 7.14, 5.26, 4.0, and 5.22 M, and Vmax values were 0.05, 0.035, 0.027 and 0.021 mg/ml/min, respectively. The kinetic values suggested that activity of enzyme was enhanced in the presence of dihydropyrimidine derivative.

Date	2009-03-20T08:13:34Z 2009-03-20T08:13:34Z 2006

Type	Article

Identifier	0301-1208 http://hdl.handle.net/123456789/3412

Language	en_US

Publisher	CSIR

Source	IJBB Vol.43(6) [December 2006]

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