Abstract
Horse‐liver alcohol dehydrogenase has been dissociated and denatured by 6 M gaunidinium hydrochloride. Removal of the denaturat under optimum conditions of the solvent leads to partial reactivation.The concentrations of the enzyme, as well as the coenzyme (NAD+ and Zn2+, affect the reactivation significantly, since high concentrations promote the formation of inactive aggregation products.Analyzing the kinetics of reactivation and reassociation, conditions far from equilibrium of dissociation‐association provide maximum yieldddd (∼ 70%). The sigmoidal kineic traces suggest a superposition of first‐order transconformation and‐second‐order association reactions; the latter are corrobosrated by the concentration dependence of thereactivation reaction.The coenzyme, NAD+, had no the kinetics of reactivation. Addition of Zn2+ leads to a significant decrease of the rate and yield of ractivation.The process of renaturation, as reflected by the regain of navive fluorescence show complex kinetics: rapid relaxations are followed by slower first‐order and secon‐order processes which parallel reactivtion.
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Dates
Type | When |
---|---|
Created | 20 years, 5 months ago (March 3, 2005, 1:52 p.m.) |
Deposited | 1 year, 9 months ago (Nov. 23, 2023, 7:17 a.m.) |
Indexed | 1 year, 9 months ago (Nov. 23, 2023, 11:40 a.m.) |
Issued | 47 years, 1 month ago (July 1, 1978) |
Published | 47 years, 1 month ago (July 1, 1978) |
Published Online | 17 years, 1 month ago (June 28, 2008) |
Published Print | 47 years, 1 month ago (July 1, 1978) |
@article{GERSCHITZ_1978, title={Refolding and Reactivation of Liver Alcohol Dehydrogenase after Dissociation and Denaturation in 6M Guanidine Hydrochloride}, volume={87}, ISSN={1432-1033}, url={http://dx.doi.org/10.1111/j.1432-1033.1978.tb12411.x}, DOI={10.1111/j.1432-1033.1978.tb12411.x}, number={3}, journal={European Journal of Biochemistry}, publisher={Wiley}, author={GERSCHITZ, Johan and RUDOLPH, Rainer and JAENICKE, Rainer}, year={1978}, month=jul, pages={591–599} }