Refolding of triose phosphate isomerase

The refolding and reactivation of the glycolytic enzyme triose phosphate isomerase (EC 5.3.1.1) has been studied. The enzyme, which is a dimer, is disaggregated and unfolded in solutions of guanidinium chloride. Unfolding, followed by changes in E(233), took place quite rapidly in 3m-guanidinium chl...

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Veröffentlicht in:	Biochemical journal 1973-09, Vol.135 (1), p.165-172
1. Verfasser:	Waley, S G
Format:	Artikel
Sprache:	eng
Schlagworte:	Animals Carbohydrate Epimerases Chickens Enzyme Activation - drug effects Guanidines Half-Life Hydrogen-Ion Concentration Kinetics Organophosphorus Compounds Osmolar Concentration Proteins Rabbits Spectrum Analysis Subtilisins Trioses
Online-Zugang:	Volltext
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