Inactivation of glyceraldehyde-3-phosphate dehydrogenase with SH-reagents and its relationship to the protein quaternary structure.

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dc.contributor.authorMalhotra, O Pen_US
dc.contributor.authorSrivastava, D Ken_US
dc.contributor.authorKayastha, A Men_US
dc.contributor.authorSrinivasan,en_US
dc.date.accessioned1993-10-01en_US
dc.date.accessioned2009-05-27T09:25:42Z
dc.date.available1993-10-01en_US
dc.date.available2009-05-27T09:25:42Z
dc.date.issued1993-10-01en_US
dc.description.abstractInactivation of mung bean glyceraldehyde-3-phosphate dehydrogenase (GPDH) with excess iodoacetate or N-ethylmaleimide exhibits pseudo-first order kinetics at pH 7.3 and 8.6 in the absence and presence of NAD+, suggesting that all the reactive SH groups (four per tetrameric GPDH molecule) have equivalent reactivity towards these reagents. This is similar to the D2-symmetry conformation proposed on the basis of thermal inactivation data [Malhotra and Srinivasan, Arch. Biochem. Biophys. 236, 775-781 (1985)]. With p-chloromercury benzoate (p-CMB), the inactivation of GPDH is very fast and its kinetics can be monitored at low reagent concentration only. Keeping a high molar p-CMB: enzyme ratio (= 47), the kinetics were found to be biphasic, with half of the activity being lost in a fast and the remaining in a slow phase, characteristic of C2-symmetry conformation and half site reactivity. The p-CMB inactivation could be largely reversed on the addition of excess cysteine. A comparison of these data with literature reports on this and other GPDHs reveals that all reagents having large non-polar moieties exhibit half site reactivity with this enzyme.en_US
dc.description.affiliationDepartment of Chemistry, Banaras Hindu University, Varanasi.en_US
dc.identifier.citationMalhotra OP, Srivastava DK, Kayastha AM, Srinivasan . Inactivation of glyceraldehyde-3-phosphate dehydrogenase with SH-reagents and its relationship to the protein quaternary structure. Indian Journal of Biochemistry & Biophysics. 1993 Oct; 30(5): 264-9en_US
dc.identifier.urihttps://imsear.searo.who.int/handle/123456789/27476
dc.language.isoengen_US
dc.source.urihttps://https://www.niscair.res.in/ScienceCommunication/ResearchJournals/rejour/ijbb/ijbb0.aspen_US
dc.subject.meshAnimalsen_US
dc.subject.meshChloromercuribenzoates --pharmacologyen_US
dc.subject.meshEthylmaleimide --pharmacologyen_US
dc.subject.meshFabaceae --enzymologyen_US
dc.subject.meshGlyceraldehyde-3-Phosphate Dehydrogenases --antagonists & inhibitorsen_US
dc.subject.meshKineticsen_US
dc.subject.meshPlants --enzymologyen_US
dc.subject.meshPlants, Medicinalen_US
dc.subject.meshProtein Conformationen_US
dc.subject.meshRabbitsen_US
dc.subject.meshRatsen_US
dc.subject.meshSaccharomyces cerevisiae --enzymologyen_US
dc.subject.meshSulfhydryl Reagents --pharmacologyen_US
dc.subject.meshSwineen_US
dc.subject.meshp-Chloromercuribenzoic Aciden_US
dc.titleInactivation of glyceraldehyde-3-phosphate dehydrogenase with SH-reagents and its relationship to the protein quaternary structure.en_US
dc.typeJournal Articleen_US
dc.typeResearch Support, Non-U.S. Gov'ten_US
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