Effect of proline on thermal inactivation, denaturation and aggregation of glycogen phosphorylase b from rabbit skeletal muscle.
It has been shown that the relatively low concentrations of proline (0.1 M) have a slight accelerating effect on thermal aggregation of glycogen phosphorylase b (Phb) from rabbit skeletal muscle registered by the accumulaton of the aggregated protein. The suppression of Phb aggregation at high proline concentrations is mainly due to the protective action of proline on the stage of unfolding of the Phb molecule. The enhancement of Phb stability in the presence of the high concentrations of proline was demonstrated by the data on differential scanning calorimetry, analytical ultracentrifugation and thermoinactivation kinetics. The construction of the protein aggregate size versus time plots allowed the acceleration of the stage of Phb aggregation in the presence of high concentrations of proline to be demonstrated. The obtained results are consistent with the predictions of the crowding theory.
Eronina
Tatyana B
TB
Bach Institute of Biochemistry, Russian Academy of Sciences, Moscow, Russia. eronina@inbi.ras.ru
Chebotareva
Natalia A
NA
Bazhina
Svetlana G
SG
Makeeva
Valentina F
VF
Kleymenov
Sergey Yu
SY
Kurganov
Boris I
BI
D000818:Animals; D002152:Calorimetry, Differential Scanning; D004305:Dose-Response Relationship, Drug; D004789:Enzyme Activation / Q000187:drug effects; D024982:Glycogen Phosphorylase, Muscle Form / Q000737:chemistry* / Q000378:metabolism*; D006358:Hot Temperature; D018482:Muscle, Skeletal / Q000201:enzymology*; D011392:Proline / Q000378:metabolism / Q000494:pharmacology*; D011485:Protein Binding / Q000187:drug effects; D011489:Protein Denaturation / Q000187:drug effects; D011817:Rabbits; D012542:Scattering, Radiation; D014461:Ultracentrifugation
D011392:Proline; D024982:Glycogen Phosphorylase, Muscle Form