Cryoinactivation and conformational drift of glyceraldehyde-3-phosphate dehydrogenase from rabbit muscle

Authors
Citation
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
Citations number
13
Categorie Soggetti
Biochemistry & Biophysics
Journal title
BIOLOGICAL CHEMISTRY
ISSN journal
14316730 → ACNP
Volume
379
Issue
11
Year of publication
1998
Pages
1319 - 1322
Database
ISI
SICI code
1431-6730(199811)379:11<1319:CACDOG>2.0.ZU;2-6
Abstract
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).