Please use this identifier to cite or link to this item: http://nopr.niscair.res.in/handle/123456789/15210
Title: Purification and characterization of 3-phosphoglycerate kinase from Ehrlich ascites carcinoma cells
Authors: Mukherjee, Kasturi
Ghosh, Swapna
Ray, Manju
Ray, Subhankar
Issue Date: Oct-2002
Publisher: NISCAIR-CSIR, India
Abstract: 3-Phosphoglycerate kinase (3-PGK) has been purified to apparent  homogeneity from Ehrlich ascites carcinoma (EAC) cells by (NH4)2SO4  precipitation, gel filtration and ion-exchange chromatography. The enzyme has been partially characterized and compared with the characteristics of this enzyme of other normal and malignant cells. The EAC cell 3-PGK is composed of a single subunit of 47 kDa. It has a broad pH optimum (pH 6.0-7.5) for it s enzymatic activity. The apparent Km values of  3-phosphoglycerate (3-PGA) and ATP for 3-PGK have been found out to be 0.25 mM and 0.1 mM respectively. Similar to 3-PGK of other cells, the EAC enzyme requires either Mg2+ or Mn2+ for full activity; the optimum concentrations of Mg2+ and Mn2+ are 0.8 mM and 0.5 mM respectively. When ATP and 3-PGA act as substrates, ADP, the  reaction product of 3-PGK-catalyzed reaction has been found to inhibit this enzyme. Kinetic studies were made on the inhibition of ADP in presence of the substrates ATP and 3-PGA. Attempts to hybridize 3-PGK and glyceraldehyde 3-phosphate dehydrogenase of EAC cells by NAD or glutaraldehyde were unsuccessful.
Page(s): 332-341
URI: http://hdl.handle.net/123456789/15210
ISSN: 0975-0959 (Online); 0301-1208 (Print)
Appears in Collections:IJBB Vol.39(5) [October 2002]

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