The effect of detergents on bovine XXXX : a kinetic approach.

@entity6000 @entity21304 @entity658 @entity10940 @entity9266
(1) Investigation of the relationship between the detergent concentration and steady-state and pre-steady-state kinetics of @entity21304 proved to be a valid approach in the study of protein-detergent interaction. (2) @entity10940 , @entity658 and @entity6000 influenced the kinetics of @entity21304 cooperatively at detergent concentrations near their critical micelle concentration. This mode of interaction reflects disaggregation of the oxidase as a result of cooperative binding of the detergent. (3) Addition of increasing concentrations of @entity9266 to the aggregated enzyme caused a more gradual decrease in aggregation of the oxidase, which did not result in a change in activity of the enzyme. This suggests that aggregation of @entity21304 occurs in a highly regular manner in which no catalytic sites are shielded off. (4) Oxidase aggregates present at detergent concentrations below the critical micelle concentration of @entity10940 and @entity6000 showed considerable activity. Their kinetics were equal to those of the oxidase in @entity9266 , suggesting that the protein molecules are aligned in a similar way in all oligomers. Aggregates present in low concentrations of @entity658 showed turnover rates that were twice as low as those observed with other aggregates. (5) Solubilisation of the oxidase by @entity658 or @entity6000 resulted in almost complete inhibition of enzymic activity, whereas the association rate of ferrocytochrome c was almost equal to that found for monomeric oxidase in laurylmaltoside. These results are in agreement with a mixed-type inhibition.
