Study of kinetics of thermal aggregation of mitochondrial aspartate aminotransferase by dynamic light scattering: protective effect of α-crystallin

被引:0
作者
Nikolay V. Golub
Kira A. Markossian
Mikhail V. Sholukh
Konstantin O. Muranov
Boris I. Kurganov
机构
[1] Russian Academy of Sciences,Bach Institute of Biochemistry
[2] Belarusian State University,Emanuel Institute of Biochemical Physics
[3] Russian Academy of Sciences,undefined
来源
European Biophysics Journal | 2009年 / 38卷
关键词
Mitochondrial aspartate aminotransferase; Aggregation; α-Crystallin; Dynamic light scattering;
D O I
暂无
中图分类号
学科分类号
摘要
Thermal aggregation of aspartate aminotransferase from pig heart mitochondria (mAAT) has been studied at various temperatures and various protein concentrations by dynamic light scattering. The character of the dependence of protein aggregate size on time indicates that aggregation of mAAT proceeds in the regime of diffusion-limited cluster–cluster aggregation. Suppression of mAAT aggregation by α-crystallin is due to transition of the aggregation process into the regime of reaction-limited cluster–cluster aggregation. Realization of this regime of aggregation means that the sticking probability for the colliding particles is less than unity.
引用
收藏
页码:547 / 556
页数:9
相关论文
共 182 条
[1]  
Abgar S(2001)Study of the chaperoning mechanism of bovine lens alpha-crystallin, a member of the alpha small heat shock superfamily Biophys J 80 1986-1995
[2]  
Vanhoudt J(1995)Self-similarity properties of alpha-crystallin supramolecular aggregates Biophys J 69 2720-2727
[3]  
Aerts T(1998)Kinetic properties and thermal stabilities of mutant forms of mitochondrial aspartate aminotransferase Biochim Biophys Acta 1386 29-38
[4]  
Clauwaert J(1987)Universal kinetics in reaction-limited aggregation Phys Rev Lett 58 274-277
[5]  
Andreasi Bassi F(1976)Large-scale purification and some properties of the mitochondrial aspartate aminotransferase from pig heart Eur J Biochem 64 519-526
[6]  
Arcovito G(2005)Relation between aggregation kinetics and the structure of kaolinite aggregates Langmuir 21 1223-1229
[7]  
De Spirito M(2003)A peptide sequence -YSGVCHTDLHAWHGDWPLPVK- [40–60] in yeast alcohol dehydrogenase prevents the aggregation of denatured substrate proteins Biochem Biophys Res Commun 307 1-7
[8]  
Mordente A(1961)The intracellular distribution, latency and electrophoretic mobility of Biochem J 81 434-441
[9]  
Martorana GE(2000)-glutamate-oxaloacetate transaminase from rat liver Biochem Biophys Res Commun 268 426-432
[10]  
Azzariti A(1979)Correlation between the chaperone-like activity and aggregate size of alpha-crystallin with increasing temperature Int J Pept Protein Res 13 409-417