【摘要】 在pH2.36的BR介质中,甲基蓝与蛋白质相互作用生成复合物,使最大波长350nm的共振光散射光谱得到增强,增强程度与蛋白质浓度成正比。据此建立了测定蛋白质的新方法。人血清白蛋白、牛血清白蛋白的线性范围分别为0～2.4mg/L、0～2.8mg/L,相应检出限分别为39.3、43.4μg/L。方法的稳定性好,灵敏度高,用于牛奶、豆浆、人血清、尿液中总蛋白质的测定,结果与考马斯亮蓝法一致。更多还原

【Abstract】 In Britton-Robinson buffer of pH2.36, the binding reaction of methyl blue with proteins enhances remarkably theresonance Rayleigh light-scattering (RLS) signal at maximum wavelength of 350 nm and forms complexes. It is found that theenhanced RLS intensities are in proportion to the concentrations of protein. Based on this, a new method for the determinationof proteins using methyl blue as indicator has been developed. Bovine serum albumin and human serum albumin could be determinedunder optimum conditions。The linear ranges of the calibration curves were 0～2.4mg/L for human serum albumin and 0～2.8mg/L for bovine serum albumin, and the detection limits were 39.3 and 43.4μg/L, respectively. The method had the advantagesof simplicity and high sensitivity. It has been used to determine total proteins in milk, soybean milk, human serum albumin andhuman urine. The results by this method are consistent with those obtained by the Coomassie brilliant blue G-250 assay。更多还原