Dithiothreitol decreases the thermal stability and unfoldingcooperativity of ribulose-1, 5-bisphosphate carboxylase/oxygenase

编号 zgly0000311589

文献类型 期刊论文

文献题名 Dithiothreitol decreases the thermal stability and unfoldingcooperativity of ribulose-1, 5-bisphosphate carboxylase/oxygenase

作者 LIGuofu  MAOHaibin  LIDonghai  GONGYandao  ZHANGXiufang  ZHAONanming 

作者单位 StateKeyLaboratoryofBiomembraneandMembraneBiotechnology  DepartmentofBiologicalSciencesandBiotechnolo 

母体文献 Progress in Natural Science;自然科学进展: 英文版 

年卷期 2003,13(3)

页码 196-200

年份 2003 

分类号 Q946.5 

关键词 二硫苏糖醇  核酮糖-1  5-二磷酸羟化/加氧酶  热稳定性  热扩散  协同效应  植物生物化学 

文摘内容 Plant rubisco consists of eight large subunits (55 kD) encoded by chloroplast gene and eight small subunits (15 kD) en-coded by nuclear gene. There are abundant cysteine residues that do not form disulfide bonds in native rubisco. Differential scanningcalorimetry has been used to study some plant rubisco and suggested an irreversible two-state denaturation due to the high cooperativity insubunits. By comparing the data from circular dichroism, fluorescence, differential scanning calorimetry, SDS electrophoresis, and activityassays in the absence or presence of DTT, we suggest that the formation of disulfide bonds in subunits during the early thermal unfolding may increase the thermal stability and the thermal unfolding cooperativity of rubisco。