Pressure inactivation of tetrameric lactate dehydrogenase homologues of confamilial deep-living fishes

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The susceptibility to inactivation by hydrostatic pressure of the tetrameric (Fig. 1) muscletype (M4) lactate dehydrogenase homologues (LDH, EC;l-lactate: NAD+ oxidoreductase) from six confamilial macrourid fishes was compared at 4 °C. These marine teleost fishes occur over depths of 260 to 4815 m. The pressures necessary to half-inactivate the LDH homologues are related to the pressures which the enzymes are exposed to in vivo (Table 1); higher hydrostatic pressures are required to inactivate the LDH homologues of the deeper-occurring macrourids. The resistance of the LDH homologues to inactivation by pressure is affected by protein concentration (Fig. 3). After an hour of incubation at pressure, the percent remaining activity approaches an asymptotic value (Fig. 2). The inactivation of the macrourid LDH homologues by pressure was not fully reversible. Assuming that inactivation by pressure was due to dissociation of the native tetramer to monomers, apparent equilibrium constants (Keq) were calculated. Volume changes (ΔV) were calculated over the range of pressures for which plots in Keq versus pressure were linear (Fig. 4). The ΔV of dissociation values of the macrourid homologues range from -219 to -439 ml mol-1 (Table 1). Although the hydrostatic pressures required to inactivate the LDH homologues of the macrourid fishes are greater than those which the enzymes are exposed to in vivo, the pressure-stability of these enzymes may reflect the resistance of these enzymes to pressure-enhanced proteolysis in vivo. © 1985 Springer-Verlag.

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Journal of Comparative Physiology B

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