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Presence of bound substrate in lactate dehydrogenase from carp liver

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Title Presence of bound substrate in lactate dehydrogenase from carp liver
 
Creator Banerjee, Nupur
Bhattacharyya, Debasish
 
Subject Carp liver enzymes
Substrate bound lactate dehydrogenase
Epimerase-lactate dehydrogenase association
Protein-ligand interaction
 
Description 182-188
While attempting to purify UDP-galactose 4-epimerase from carp liver
extract at pH 8.0, it was observed that the preparation even after dialysis
could reduce NAD to NADH, interfering epimerase assay. The NAD reduction
activity and the epimerase were co-eluted in a series of chromatographic steps.
Mass spectrometric analysis of semi-purified fraction revealed that carp liver
lactate dehydrogenase (LDH) contained bound lactate which was converted to pyruvate
in the presence of NAD. The enzyme-bound lactate and the association with
epimerase stabilized LDH from trypsin digestion and thermal inactivation at 45°C by factors of 2.7 and 4.2 respectively, as compared to
substrate-free LDH. LDH and epimerase do not belong
to any one pathway, but are the rate-limiting enzymes of two different pathways
of carbohydrate metabolism. Typically, strongly associated enzymes work in
combination, such as two enzymes of the same metabolic pathway. In that
background, co-purification of LDH and epimerase as reloaded in this study was
an unusual phenomenon.
 
Date 2012-06-18T11:33:11Z
2012-06-18T11:33:11Z
2012-06
 
Type Article
 
Identifier 0975-0959 (Online); 0301-1208 (Print)
http://hdl.handle.net/123456789/14278
 
Language en_US
 
Rights CC Attribution-Noncommercial-No Derivative Works 2.5 India
 
Publisher NISCAIR-CSIR, India
 
Source IJBB Vol.49(3) [June 2012]