Effect of alpha-crystallin on thermal denaturation and aggregation of rabbit muscle glyceraldehyde-3-phosphate dehydrogenase.
The study of thermal denaturation of rabbit muscle glyceraldehyde-3-phosphate dehydrogenase (GAPDH) in the presence of alpha-crystallin by differential scanning calorimetry (DSC) showed that the position of the maximum on the DSC profile (T(max)) was shifted toward lower temperatures with increasing alpha-crystallin concentration. The diminishing GAPDH stability in the presence of alpha-crystallin has been explained assuming that heating of GAPDH induces dissociation of the tetrameric form of the enzyme into dimers interacting with alpha-crystallin. The dissociation of the enzyme tetramer was shown by sedimentation velocity at 45 degrees C. Suppression of thermal aggregation of GAPDH by alpha-crystallin was studied by dynamic light scattering under the conditions wherein temperature was elevated at a constant rate. The construction of the light scattering intensity versus the hydrodynamic radius (R(h)) plots enabled estimating the hydrodynamic radius of the start aggregates (R(h,0)). When aggregation of GAPDH was studied in the presence of alpha-crystallin, the start aggregates of lesser size were observed.
Khanova
Helen A
HA
Bach Institute of Biochemistry, Russian Academy of Sciences, Moscow, Russia.
Markossian
Kira A
KA
Kleimenov
Sergey Yu
SY
Levitsky
Dmitrii I
DI
Chebotareva
Natalia A
NA
Golub
Nikolay V
NV
Asryants
Regina A
RA
Muronetz
Vladimir I
VI
Saso
Luciano
L
Yudin
Igor K
IK
Muranov
Konstantin O
KO
Ostrovsky
Michail A
MA
Kurganov
Boris I
BI
D000818:Animals; D002152:Calorimetry, Differential Scanning; D019281:Dimerization; D004795:Enzyme Stability; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases / Q000737:chemistry* / Q000378:metabolism; D009132:Muscles / Q000201:enzymology*; D011487:Protein Conformation; D011489:Protein Denaturation; D011817:Rabbits; D013696:Temperature; D038201:alpha-Crystallins
D038201:alpha-Crystallins; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases