[Regulation of the supramolecular structure and catalytic activity of D-glyceraldehyde-3-phosphate dehydrogenase in systems of reversed Aerosol OT micelles in octane].
Reversible formation of various oligomeric forms of rabbit skeletal muscle D-glyceraldehyde-3-phosphate dehydrogenase (GAPD) in reversed micelles of Aerosol OT in octane at variable degrees of hydration (size) of the micelles, has been demonstrated. All the oligomeric forms of the enzyme possess a catalytic activity in the reversed micelle system. Data from the sedimentation analysis provide evidence for the formation of a monomer, a dimer and a tetramer of GAPD. The peculiarities of the structure of oligomeric forms of the enzyme revealed in fluorescence studied are discussed.
Kliachko
N L
NL
Ugol'nikova
A V
AV
Ivanov
M V
MV
Levashov
A V
AV
D000818:Animals; D002384:Catalysis; D004143:Dioctyl Sulfosuccinic Acid; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases / Q000737:chemistry / Q000378:metabolism*; D007700:Kinetics; D008823:Micelles; D018482:Muscle, Skeletal / Q000201:enzymology; D009795:Octanes; D011487:Protein Conformation; D011817:Rabbits; D013050:Spectrometry, Fluorescence
D008823:Micelles; D009795:Octanes; D004143:Dioctyl Sulfosuccinic Acid; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases; C026728:octane
Reguliatsiia nadmolekuliarnoĭ struktury i kataliticheskoĭ aktivnosti D-glitseral'degid-3-fosfatdegidrogenazy v sistemakh obrashchennykh mitsell aérozolia OT v oktane.