Competitive Inhibition of Enzyme Activity by Urea

Competitive Inhibition of Enzyme Activity by Urea*

It is widely accepted that urea and guanidine act as protein denaturants by breaking intramolecular hydrogen bonds (1). Loss of catalytic activity in the presence of urea is thought to occur by elimination of bonds contributing to the tertiary structure of enzyme molecules. Subsequent restoration of structural and catalytic properties by removal of the denaturant, “reversible denaturation,” is ...

Competitive inhibition of enzyme activity by urea.

It is widely accepted that urea and guanidine act as protein denaturants by breaking intramolecular hydrogen bonds (1). Loss of catalytic activity in the presence of urea is thought to occur by elimination of bonds contributing to the tertiary structure of enzyme molecules. Subsequent restoration of structural and catalytic properties by removal of the denaturant, “reversible denaturation,” is ...

Inhibition of urea-cycle activity by high concentrations of alanine.

1. Conditions are described in which high intracellular alanine concentrations inhibit urea-cycle flux in isolated hepatocytes. 2. Inhibition of urea-cycle flux by added alanine is DL-cycloserine-insensitive and is accompanied by an increase in intracellular citrulline and a decrease in ornithine. 3. Argininosuccinate synthetase (EC 6.3.4.5) activity in rat liver cytosol is inhibited by alanine...

Enzyme-Linked Immunosorbent Assay Competitive Binding Inhibition

The competitive inhibition of the urease-catalyzed hydrolysis of urea by phosphate.

It follows from equation (1) that when l/u is plotted (usually as the ordinate) against l/s a straight line will be obtained with inhibitory action influencing either the slope or the ordinate intercept or both. Thus the type of inhibition may be defined on the basis of the effect of the inhibitory action upon the slope and intercept in the above plot. In the absence of an inhibitor (i = 0) equ...