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Purification and characterization of 3-phosphoglycerate kinase from Ehrlich ascites carcinoma cells

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Title Purification and characterization of 3-phosphoglycerate kinase from Ehrlich ascites carcinoma cells
 
Creator Mukherjee, Kasturi
Ghosh, Swapna
Ray, Manju
Ray, Subhankar
 
Description 332-341
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.
 
Date 2012-12-08T16:13:48Z
2012-12-08T16:13:48Z
2002-10
 
Type Article
 
Identifier 0975-0959 (Online); 0301-1208 (Print)
http://hdl.handle.net/123456789/15210
 
Language en_US
 
Rights CC Attribution-Noncommercial-No Derivative Works 2.5 India
 
Publisher NISCAIR-CSIR, India
 
Source IJBB Vol.39(5) [October 2002]