Effect of thermodynamic nonideality in kinetic studies: Evidence for reversible unfolding of urease during urea hydrolysis

A combination of enzyme kinetic studies and active enzyme gel chromatography on Sepharose CL-6B was used to explore conformational changes of the enzyme urease as it catalyzes the hydrolysis of urea in 0.7 m phosphate buffer, pH 7.0, at 20 °C. It is shown that elucidation of this system is only poss...

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Veröffentlicht in:	Archives of biochemistry and biophysics 1985-05, Vol.239 (1), p.147-154
Hauptverfasser:	Nichol, Lawrence W., Owen, Elisabeth A., Winzor, Donald J.
Format:	Artikel
Sprache:	eng
Schlagworte:	Analytical, structural and metabolic biochemistry Biological and medical sciences Enzyme Activation Enzymes and enzyme inhibitors Fundamental and applied biological sciences. Psychology Hydrolases Hydrolysis In Vitro Techniques Kinetics Models, Biological Molecular Conformation Substrate Specificity Thermodynamics Urea - metabolism Urease - metabolism
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