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Limited proteolysis of maize NADP-malic enzyme

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Title Limited proteolysis of maize NADP-malic enzyme
 
Creator Pinto, S
Rao, S R
Bhagwat, A S
 
Description 382-389
The incubation of maize malic enzyme at 37°C
with trypsin at a ratio of 150:1 of malic enzyme to trypsin caused rapid and complete
in activation of enzyme activity. The inactivation was caused by fairly specific
cleavage or the enzyme monomer (62 kDa) into 40 kDa and 20 kDa fragments. The intensity
of 40 kDa band increased with the time of treatment of enzyme with trypsin from
2 to 30 min. Substrates, especially NADP (25μM) provided almost total protection
against trypsin inactivation of the enzyme activity. The studies carried out with
various other endoproteases indicated that endoprotease Lys-C was most effective
in inactivating malic enzyme activity. The kinetic properties of the truncated

enzyme have been studied. The Km
value for malate in case of native and modified enzyme was found to be identical.
Km NADP for the modified enzyme was slightly higher indicating
that after proteolysis the enzyme affinity for NADP had decreased. Limited proteolysis
with trypsin did not show any appreciable change in fluorescence properties of the
modified

enzyme. Binding of NADPH to the enzyme was
not affected after modification.
 
Date 2013-07-15T09:35:42Z
2013-07-15T09:35:42Z
2002-12
 
Type Article
 
Identifier 0975-0959 (Online); 0301-1208 (Print)
http://hdl.handle.net/123456789/19782
 
Language en_US
 
Rights CC Attribution-Noncommercial-No Derivative Works 2.5 India
 
Publisher NISCAIR-CSIR, India
 
Source IJBB Vol.39(6) [December 2002]