Sm. Tian et Kc. Ruan, Cryoinactivation and conformational drift of glyceraldehyde-3-phosphate dehydrogenase from rabbit muscle, BIOL CHEM, 379(11), 1998, pp. 1319-1322
The cryoinactivation of glyceraldehyde-3-phosphate dehydrogenase from rabbi
t muscle (GAPDH-rabbit) was studied. It was found that the inactivation of
GAPDH-rabbit at 0 degrees C was much faster than that of GAPDH from yeasts,
and showed obvious time and concentration dependence. The spectral propert
ies, enzyme activity and behavior under pressure, of GAPDH-rabbit treated e
ither by cryoinactivation, or pressure-induced dissociation and reassociati
on, were very similar. These results provided evidence to support the idea
that cryoinactivation of oligomeric proteins, might take place through a cy
cle of dissociation-reassociation accompanied with the so-called conformati
onal drift postulated by King and Weber (1986).