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Conformational drift of dissociated lactate dehydrogenases.

Bovine and porcine lactate dehydrogenases, in solutions of 0.1-10 microM at neutral pH, dissociate into monomers upon application of hydrostatic pressures of up to 2 kbar. The dissociation was determined from observations of the polarization of fluorescence under pressure in seeming equilibrium conditions and by occasional hybridization experiments of the H4 and M4 isozymes. Decompression is followed by the rapid association of the monomers into tetramers and by slow, and sometimes incomplete, return of the enzymic activity. The dissociation curves obtained on compression and decompression differ, indicating that association results in partial loss of subunit affinity. These phenomena are attributed to a slow conformational drift that follows the loss of contact of the monomers with each other and to an even slower reversal of the drift that takes place upon reassociation.