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    人血清蛋白的共振散射光谱法测定

    RESONANCE SCATTERING SPECTROMETRIC DETERMINATION OF HUMAN SERUM ALBUMIN

    • 摘要: 在pH 7.0的缓冲介质中,吖啶黄(AO)与人血清蛋白(HSA)通过静电引力生成离子缔合物.与单独吖啶黄在相同溶液条件下相比,其共振散射光谱的强度有显著增强.在362 nm波长下所测得共振散射光谱峰的强度值与HSA的浓度值在0-1.3 mg·L-1范围内呈线性关系,并求得其检出限为32 μg·L-1.上述反应条件已用于试样中HSA的测定.

       

      Abstract: It was found that in a buffer solution of pH 7.0,an electrostatic association compound was formed between human serum albumin (HSA) and acridine orange (AO),leading to a remarkable enhancement of the intensity of resonance scattering spectra measured at 362 nm.Linear relationship between the values of ΔI (Δ=I-I0,where I0 is the intensity of the spectral peak without adding HSA) and values of concentration of HSA was obtained in the range of 0 to 1.3 mg·L-1 of HSA,with a detection limit of 32 μg·L-1.The above reaction conditions were used in the determination of HSA.

       

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