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http://nopr.niscpr.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 |
| ISSN: | 0975-0959 (Online); 0301-1208 (Print) |
| Appears in Collections: | IJBB Vol.39(5) [October 2002] |
Files in This Item:
| File | Description | Size | Format | |
|---|---|---|---|---|
| IJBB 39(5) 332-341.pdf | 2.15 MB | Adobe PDF | View/Open |
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