Please use this identifier to cite or link to this item: http://nopr.niscair.res.in/handle/123456789/3412
Title: Purification of L-asparaginase from a bacteria Erwinia carotovora and effect of a dihydropyrimidine derivative on some of its kinetic parameters
Authors: Kamble, V P
Rao, R Srinivasa
Borkar, Prita S
Keywords: Erwinia carotovora
L-Asparaginase activity
Dihydropyrimidine derivative
Issue Date: 2006
Publisher: CSIR
Abstract: 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.
Description: 391-394
URI: http://hdl.handle.net/123456789/3412
ISSN: 0301-1208
Appears in Collections:IJBB Vol.43(6) [December 2006]

Files in This Item:
File Description SizeFormat 
IJBB 43(6) 391-394.pdf70.69 kBAdobe PDFView/Open


Items in NOPR are protected by copyright, with all rights reserved, unless otherwise indicated.