[The effect of hydrophobization of glucose-6-phosphate dehydrogenase with progesterone on its thermal inactivation].
Thermal inactivation of glucose-6-phosphate dehydrogenase (G6PDH) and its conjugates with progesterone containing 3, 7 and 35 molecules of the modifier was studied in bidistilled water over a temperature range 35-47 degrees. At different temperatures and initial concentrations of the enzyme and its modified forms, thermal inactivation is described by the equation of the first order up to a significant degree of enzyme deactivation. The effective Kin values are decreased with the increase of the native G6PDH concentration and changed in a complicated manner with the increase of the conjugate concentration depending on the enzyme modification degree, which reflects a great role of the enzyme hydrophobicity in its inactivation. The role of hydrophobicity of the modified G6PDH in changes of its specific activity is discussed.
Karaseva
E I
EI
Eremin
A N
AN
Metelitsa
D I
DI
D004795:Enzyme Stability; D005954:Glucosephosphate Dehydrogenase / Q000037:antagonists & inhibitors*; D006358:Hot Temperature; D066298:In Vitro Techniques; D007700:Kinetics; D011374:Progesterone / Q000494:pharmacology*
D011374:Progesterone; D005954:Glucosephosphate Dehydrogenase
Vliianie gidrofobizatsii gliukozo-6-fosfatdegidrogenazy progesteronom na ee termicheskuiu inaktivatsiiu.