Effect of 2-hydroxypropyl-β-cyclodextrin on thermal inactivation, denaturation and aggregation of glyceraldehyde-3-phosphate dehydrogenase from rabbit skeletal muscle

被引：14
作者：
Maloletkina, Olga I. [1 ]
Markossian, Kira A. [1 ]
Asryants, Regina A. [2 ,3 ]
Semenyuk, Pavel I. [2 ,3 ]
Makeeva, Valentina F. [1 ]
Kurganov, Boris I. [1 ]
机构：
[1] Russian Acad Sci, Bach Inst Biochem, Moscow 119071, Russia
[2] Moscow MV Lomonosov State Univ, Belozersky Inst Phys Chem Biol, Moscow, Russia
[3] Moscow MV Lomonosov State Univ, Fac Bioengn & Bioinformat, Moscow, Russia
来源：
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES | 2010年 / 46卷 / 05期
基金：
俄罗斯基础研究基金会;
关键词：
Glyceraldehyde-3-phosphate; dehydrogenase; 2-Hydroxypropyl-beta-cyclodextrin; Aggregation; ALPHA-CRYSTALLIN; AQUEOUS-SOLUTION; PHARMACEUTICAL APPLICATIONS; FLUORESCENCE SPECTROSCOPY; PROTEIN AGGREGATION; CIRCULAR-DICHROISM; BETA-CYCLODEXTRIN; STABILITY; MECHANISM; GROEL;
D O I：
10.1016/j.ijbiomac.2010.03.008
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：
The effect of 2-hydroxypropyl-beta-cyclodextrin (HP-beta-CD) on thermal aggregation of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) from rabbit skeletal muscle at 45 degrees C has been studied using dynamic light scattering. In the presence of HP-beta-CD higher values of the rate of aggregation and larger aggregates were registered. The acceleration of GAPDH aggregation was due to destabilization of the enzyme molecule under the action of HP-beta-CD. This is evidenced by the data on thermal inactivation of GAPDH and differential scanning calorimetry. (C) 2010 Elsevier B.V. All rights reserved.
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页码：487 / 492
页数：6
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