Effect of proline on thermal inactivation, denaturation and aggregation of glycogen phosphorylase b from rabbit skeletal muscle

被引:45
|
作者
Eronina, Tatyana B. [1 ]
Chebotareva, Natalia A. [1 ]
Bazhina, Svetlana G. [1 ]
Makeeva, Valentina F. [1 ]
Kleymenov, Sergey Yu. [2 ]
Kurganov, Boris I. [1 ]
机构
[1] Russian Acad Sci, Bach Inst Biochem, Moscow 119071, Russia
[2] Russian Acad Sci, NK Koltsov Dev Biol Inst, Moscow 119991, Russia
基金
俄罗斯基础研究基金会;
关键词
Glycogen phosphorylase b; Inactivation; Denaturation; Aggregation; Proline; ALPHA-CRYSTALLIN; ANALYTICAL ULTRACENTRIFUGATION; PROTEIN AGGREGATION; CROWDING CONDITIONS; SELF-ASSOCIATION; CREATINE-KINASE; COENZYME FORMS; FOLDING AIDS; OSMOLYTES; MECHANISM;
D O I
10.1016/j.bpc.2008.12.007
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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. (C) 2008 Elsevier B.V. All rights reserved.
引用
收藏
页码:66 / 74
页数:9
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