Change in kinetic regime of protein aggregation with temperature   increase. Thermal aggregation of rabbit muscle creatine kinase

doi:10.1134/S000629790603014X

CORC > 北京大学 > 生命科学学院

	Change in kinetic regime of protein aggregation with temperature increase. Thermal aggregation of rabbit muscle creatine kinase
	Fedurkina, NV ; Belousova, LV ; Mitskevich, LG ; Zhou, HM ; Chang, Z ; Kurganov, BI
刊名	biochemistry moscow
	2006
关键词	creatine kinase thermal aggregation kinetics small heat shock protein Hsp 16.3 MYCOBACTERIUM-TUBERCULOSIS HSP16.3 CHAPERONE-LIKE ACTIVITY CRYSTAL-STRUCTURE DENATURATION INACTIVATION DISSOCIATION MUTAGENESIS RESIDUES
DOI	10.1134/S000629790603014X
英文摘要	Creatine kinase thermal aggregation kinetics has been studied in 30 mM Hepes-NaOH buffer, pH 8.0, at two temperatures: 50.6 and 60 degrees C. Aggregation kinetics was analyzed by measuring the growth of apparent absorption (A) at 400 nm. It was found that the limiting value of apparent absorption (A(lim)) is proportional to protein concentration at both temperatures. The first order rate constant (k(I)) does not depend on protein concentration in the range 0.05-0.2 mg/ml at temperature 50.6 degrees C, but at temperature 60 degrees C it increases with the growth of protein concentration in the range 0.1-0.4 mg/ml. Kinetic curves, shown in coordinates {A/A(lim);t}, in experiments at 50.6 degrees C fuse to a common curve, which coincides with the theoretical curve of creatine kinase denaturation calculated using the denaturation rate constant determined from differential scanning calorimetry. At temperature 60 degrees C, half-transformation time t(1/2) = ln2/k(1) decreases when protein concentration grows. We conclude that when temperature increased from 50.6 to 60 degrees C, change in the kinetic regime of thermal creatine kinase aggregation took place: at 50.6 degrees C aggregation rate is limited by the stage of protein molecule denaturation, but at 60 degrees C it is limited by the stage of protein aggregate growth, which proceeds as a reaction of pseudo-first order. Small heat shock protein Hsp 16.3 Mycobacterium tuberculosis suppresses the creatine kinase aggregation.; Biochemistry & Molecular Biology; SCI(E); EI; 12; ARTICLE; 3; 325-331; 71
语种	英语
内容类型	期刊论文
源URL	[http://ir.pku.edu.cn/handle/20.500.11897/252264]
专题	生命科学学院
推荐引用方式 GB/T 7714	Fedurkina, NV,Belousova, LV,Mitskevich, LG,et al. Change in kinetic regime of protein aggregation with temperature increase. Thermal aggregation of rabbit muscle creatine kinase[J]. biochemistry moscow,2006.
APA	Fedurkina, NV,Belousova, LV,Mitskevich, LG,Zhou, HM,Chang, Z,&Kurganov, BI.(2006).Change in kinetic regime of protein aggregation with temperature increase. Thermal aggregation of rabbit muscle creatine kinase.biochemistry moscow.
MLA	Fedurkina, NV,et al."Change in kinetic regime of protein aggregation with temperature increase. Thermal aggregation of rabbit muscle creatine kinase".biochemistry moscow (2006).