摘要
通过盐析、阴离子交换层析和凝胶过滤等方法,获得一种苦荞麦种子贮藏蛋白。经非变性SDS-PAGE分析,纯化后的蛋白质纯度达到了95%以上,分子量约58kD。进一步采用荧光光谱技术,研究VB1与纯化的苦荞麦蛋白间的相互作用。结果表明,VB1与该蛋白质结合形成复合物后,内源荧光发生改变,其猝灭机制属于形成化合物所引起的静态猝灭。VB1与苦荞蛋白作用的结合常数为3.9×104L/mol,结合位点数为1。分子间的结合力主要为静电作用力。
A storage protein from tartary buckwheat seeds was purified by salting out, anion exchange chromatography and size exclusion chromatography. The interaction of thiamine with the target protein was studied by fluorescence spectroscopy. The quenching mechanism is suggested as static quenching caused by formation of new compound. The equilibrium constant is 3.9 ×10^4 L/mol. The number of binding site is 1.
出处
《食品科学》
EI
CAS
CSCD
北大核心
2008年第11期87-89,共3页
Food Science
基金
国家自然科学基金项目(30470178
30671084)
山西省自然科学基金项目(2007011077)
关键词
苦荞
VB1结合蛋白
荧光光谱
tartary buckwheat
thiamine-binding protein
fluorescence spectroscopy
