Cryoinactivation and conformational drift of glyceraldehyde-3-phosphate dehydrogenase from rabbit muscle.
The cryoinactivation of glyceraldehyde-3-phosphate dehydrogenase from rabbit 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 properties, enzyme activity and behavior under pressure, of GAPDH-rabbit treated either by cryoinactivation, or pressure-induced dissociation and reassociation, were very similar. These results provided evidence to support the idea that cryoinactivation of oligomeric proteins, might take place through a cycle of dissociation-reassociation accompanied with the so-called conformational drift postulated by King and Weber (1986).
Tian
S
S
Shanghai Institute of Biochemistry, Academia Sinica, China.
Ruan
K
K
D000818:Animals; D003080:Cold Temperature; D004789:Enzyme Activation; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases / Q000037:antagonists & inhibitors* / Q000737:chemistry* / Q000378:metabolism; D009132:Muscles / Q000201:enzymology*; D011312:Pressure; D011487:Protein Conformation; D011817:Rabbits; D012441:Saccharomyces cerevisiae / Q000201:enzymology; D013050:Spectrometry, Fluorescence; D013816:Thermodynamics
D005987:Glyceraldehyde-3-Phosphate Dehydrogenases