Refolding and Reactivation of Liver Alcohol Dehydrogenase after Dissociation and Denaturation in 6M Guanidine Hydrochloride
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منابع مشابه
Refolding of the precursor and mature forms of mitochondrial aspartate aminotransferase after guanidine hydrochloride denaturation.
The mitochondrial isozyme of aspartate aminotransferase (mAspAT), a dimeric pyridoxal phosphate (PLP)-dependent enzyme, is encoded by the nuclear genome and synthesized in the cytoplasm as a precursor protein (pmAspAT) containing a 29-residue amino-terminal signal peptide which is essential for its targeting and import into mitochondria. In the cytosolic-like environment of rabbit reticulocyte ...
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Glucose 6-phosphate dehydrogenase (G6PD) from Streptomyces aureofaciens was purified and denatured in 6 M urea. Denaturation led to complete dissociation of the enzyme into its inactive monomers, 98% loss of the enzyme activity, about 30% decrease in the protein fluorescence and a 10 nm red shift in the emission maximum. Dilution of urea-denatured enzyme resulted in regaining of the enzyme acti...
متن کاملThe behavior of horse liver alcohol dehydrogenase in guanidine hydrochloride solutions.
The z-average molecular weight of horse liver alcohol dehydrogenase in dilute neutral buffer is 78,200 by sedimentation equilibrium. Guanidine hydrochloride, 1 M, reversibly inhibits enzymatic activity. The inhibition with nicotinamide adenine dinucleotide is competitive and with ethanol is mixed. When ethylenediaminetetraacetate is added to the enzyme in 1 M guanidine hydrochloride, zinc is re...
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In 4 M guanidine hydrochloride (GdnHCl), the dimeric enzyme glucose-6-phosphate dehydrogenase from Leuconostoc mesenteroides (G6PD) dissociated to subunits and was extensively unfolded. Rapid dilution of this high GdnHCl concentration allowed G6PD to partially renature, as measured by enzyme reactivation, to a level which depended on the conditions employed. The fraction of the enzyme which did...
متن کاملDenaturation and renaturation of bovine liver glutamic dehydrogenase after dissociation in various denaturants.
Denaturation, Renaturation, Glutamic Dehydrogenase Oligomeric glutamic dehydrogenase from bovine liver is dissociated to inactive monomers (Mr = 56 000) under a wide variety of conditions: 3 > pH> 12, 6 m guanidine • HC1, 6 M urea, 0.2% sodium dodecylsulfate. High hydrostatic pressure (< 1 kbar) only affects the association equi librium of the native hexamer to higher polymers. The respective ...
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ژورنال
عنوان ژورنال: European Journal of Biochemistry
سال: 1978
ISSN: 0014-2956,1432-1033
DOI: 10.1111/j.1432-1033.1978.tb12411.x