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- W2008992054 abstract "The effect of miscible solvents and salts on the sigmoidal grace period inactivation behavior of the enzyme urease was examined at 50°C. Methanol, glycerol, and Na2SO4 stabilized whereas acetone and salts such as KNO3 and LiCl accelerated the rate of inactivation. The initial dissociation of the native urease hexamer into two trimers appears to be the rate-limiting step of the inactivation pathway under the conditions examined. Salts and solvents appear to influence dissociation kinetics by altering the hydrophobic forces that stabilize urease quaternary structure. This hypothesis is supported by the effect of the various salts on the dissociation rate followed the Hofmeister series. Aggregation of the trimer species, the second step in the inactivation pathway, was very rapid and appeared to not be strongly affected by the presence of solutes." @default.
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- W2008992054 title "Solute modulation of urease inactivation kinetics" @default.
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- W2008992054 doi "https://doi.org/10.1016/0141-0229(95)00226-x" @default.
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