摘要
分别将编码牛肝微粒体细胞色素b5水溶性结构域片段Ala7－Arg88和Ser5－Ser97基因在大肠杆菌JM83中高效表达，分离纯化后得到Tb5和Lb52种重组野生型蛋白．用核磁共振、紫外可见光谱、圆二色散光谱、循环伏安等方法研究结果表明，Lb5肚链2端残基未能使蛋白质的血红素周围环境与Tb5之间产生明显差异，但热变性和尿素变性行为的比较结果都表明Lb5较Tb5稳定，这些稳定性差异，主要由Lb5蛋白质N末端的Ser5和Lys62个残基所贡献．
Bovine liver microsomal gene encoding water-soluble heme-containing fragment of cytochrome b5 was expressed in E. coli JM83. Two recombinate wild type cytochrome Lb5 and Tb, were isolated and purified.Studies by NMR,UV-visible,Circular dichroism(CD),cyclic voltammetry (CV) etc. show that the increase of the terminal residues on Lb, did not cause significant difference of the heme pocket from the Tb5. But the study on the protein stabillty to denaturant and heat shows that the Cyt Lb, structural stability is more stable than Cyt Tb5,that can be attributed to the N-terminal residues Ser5 and Lys6 of Cyt Lb5.
出处
《复旦学报（自然科学版）》
CAS
CSCD
北大核心
1999年第6期611-616,共6页
Journal of Fudan University：Natural Science
基金
国家自然科学基金!29731030
