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Adsoptive immobilization of glutamate dehydrogenase in allosterically-activated conformation
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Z. سالمی   , M. نعمت گرگانی , F. مهنازاده |
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Abstract: (20427 Views) |
| Intoduction. Allosteric enzymes, in adcittion to their active site, contain sites for the
binding of positive and negative effector molecules which regulate the enzyme's activity.
In this research, the enzyme glutamate dehydrogenase (GDH) taken from bovine
liver, has been chosen as an allosteric model. In previous studies this enzyme was
immobilized on hexadecyl fractosil while not only maintaining its catalytic activity but
also capable of responding to various effectors. The aims of this study were to examine
the immobilization of GDH on different matrixes and the effect of PH on the activity of
the free and immobilized enzyme.
Material and Methods. Matrixes carrying a variety of ligands such as L-leucine,
D-leucine L-alanine were synthesized where upon the immobilization of GDH was
investigated. Meanwhile the effect of PH on the activity of the free and immobilized
enzyme (in the presence and absence of L-leucine was studied.
Results. The enzyme was immobilized in an active conformation and in the presence
of a positive effector. In all the pH values tested, a higher acitvity was obtained using
preparations containing palmityl grioups substituted with L-leucine.
Conclusion. It is cincluded that the allosteric enzyme is immobilized with the effector
interacting at its allosteric site. The immobilized preparation may be used in continuos
catalytic transformations |
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| Keywords: Immobilization, Glutamate dehydrogenase, Allosteric regulation, Effectors |
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Full-Text [PDF 762 kb]
(2780 Downloads)
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Type of Study: Research |
Subject:
General
Received: 2009/02/2 | Published: 1999/11/15
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