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- W2011567408 abstract "The three isozymes of mouse brain enolase (αα, αγ and γγ) were subjected to pressures between 160 MPa and 380 MPa. Enzymatic activity 2 min after the pressure exposure was used to monitor pressure‐induced changes in the physical state of the protein. Pressure caused a reversible inactivation of all three forms; αα showed a continual inactivation with increasing pressure whereas the inactivation curves for αγ and γγ were biphasic. P 1/2 for αα was 190 MPa, for αγ 210 MPa and for γγ 280 MPa. Volume changes associated with this inactivation were calculated for all three forms of the enzyme; Δ V 0 varied from – 150 ml mol −1 to – 170 ml mol −1 , assuming a model in which there was no change in the aggregation state of the enzyme, or from – 230 ml mol −1 to – 250 ml mol −1 assuming that the enzyme dissociated on exposure to pressure. The half‐time for reactivation was measured as a function of the concentration of enzyme; the results are consistent with an inactivation that is due to dissociation of the dimeric enzyme into monomers." @default.
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- W2011567408 date "1982-11-01" @default.
- W2011567408 modified "2023-09-27" @default.
- W2011567408 title "The Pressure-Induced, Reversible Inactivation of Mouse Brain Enolases" @default.
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- W2011567408 doi "https://doi.org/10.1111/j.1432-1033.1982.tb07003.x" @default.
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