摘要
在pH3．3的Britton—Robinson（B—R）缓冲溶液中，对溴甲酚绿（BCG）与牛血清白蛋白（BSA）相互作用的吸收光谱进行了初步研究。结果表明：BCG与BSA作用在室温下能迅速结合成复合物，并且随着BSA的浓度增大，在444nm处的吸收峰降低，618nm处吸收峰升高并红移至628nm。在此波长下测定其复合物的吸光度，其吸光度的增加值（△4）与BSA的质量浓度在8～260ug／mL范围内呈良好的线性关系（r=0．9996），检出限为4ug／mL。该方法应用于鲜奶粉和液态纯牛奶样品中总蛋白的测定，回收率分别为92．7％，95．5％，结果与考马斯亮蓝G250法基本一致。
The absorption spectrum of the complex of bromocresol green （BCG） and bovine serum albumin （BSA） was studied preliminarily in the Britton-Robinson （B-R） buffer solution （pH 3.3）. The results showed that BCG and BSA could react with each other and the peak intensity at 444 nm reduced, the peak intensity at 618 nm increased and the peak shifted to 628 nm. The absorbance of the complex was linearly proportional to the BSA concentration in the range of 8 - 260ug/mL, and the limit of detection was 4ug/mL. The method is simple, fast, and it has high selectivity and sensitivity. The proposed method was applied to the determination of the total protein in the fresh milk powder and liquid milk samples with satisfactory results. The experimental results are roughly identical with the results obtained by the coomassie brilliant blue G250.
出处
《分析试验室》
CAS
CSCD
北大核心
2009年第9期82-84,共3页
Chinese Journal of Analysis Laboratory
关键词
溴甲酚绿
分光光度法
牛血清白蛋白
Bromocresol green
Spectrophotometry
Bovine seruro albumin
