|
NISCAIR ONLINE PERIODICALS REPOSITORY (NOPR) >
NISCAIR PUBLICATIONS >
Research Journals >
Indian Journal of Biochemistry and Biophysics (IJBB) >
IJBB Vol.49 [2012] >
IJBB Vol.49(3) [June 2012] >
| Title: | Presence of bound substrate in lactate dehydrogenase from carp liver |
| Authors: | Banerjee, Nupur
Bhattacharyya, Debasish |
| Keywords: | Carp liver enzymes
Substrate bound lactate dehydrogenase
Epimerase-lactate dehydrogenase association
Protein-ligand interaction |
| Issue Date: | Jun-2012 |
| Publisher: | NISCAIR-CSIR, India |
| Abstract: | 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. |
| Page(s): | 182-188 |
| CC License: |  CC Attribution-Noncommercial-No Derivative Works 2.5 India |
| ISSN: | 0975-0959 (Online); 0301-1208 (Print) |
| Source: | IJBB Vol.49(3) [June 2012]
|
|
