血清白蛋白和大鼠甲胎蛋白与黄曲霉毒素B1相互作用的荧光研究。特异性和结合参数。
Fluorescence studies of the interactions of serum albumin and rat alpha1-fetoprotein with aflatoxin B1. Specificity and binding parameters.
作者信息
Evrain C, Cittanova N, Jayle M F
出版信息
Biochim Biophys Acta. 1978 Apr 26;533(2):408-14. doi: 10.1016/0005-2795(78)90386-0.
The interaction of bovine serum albumin and rat alpha1-fetoprotein with aflatoxin B1 has been followed by the fluorescence quenching of the protein in presence of the ligand. The binding parameters (n, number of sites and Kd, dissociation constant) have been determined for the bovine serum albumin-alflatoxin B1 system: n = 3.5 and Kd = 3.1 +/- 0.5 . 10(-5) M and for the alpha-fetoprotein-aflatoxin system: n = 4 and Kd = 3.7 +/-0.5 . 10(-5) M. The competition of anilino-naphthalene-sulfonate and aflatoxin B1 for the same hydrophobic sites on bovine serum albumin has been demonstrated. The fluorescence quenching of various proteins (lysozymes, egg-albumin, gamma-globulin) by aflatoxin B1 have shown that there is not a strict specificity of aflatoxin towards proteins.
在配体存在的情况下，通过蛋白质的荧光猝灭跟踪了牛血清白蛋白和大鼠甲胎蛋白与黄曲霉毒素B1的相互作用。已测定了牛血清白蛋白 - 黄曲霉毒素B1体系的结合参数（n，结合位点数；Kd，解离常数）：n = 3.5，Kd = 3.1±0.5×10⁻⁵ M；以及甲胎蛋白 - 黄曲霉毒素体系的结合参数：n = 4，Kd = 3.7±0.5×10⁻⁵ M。已证实苯胺 - 萘 - 磺酸盐和黄曲霉毒素B1对牛血清白蛋白上相同疏水位点的竞争。黄曲霉毒素B1对各种蛋白质（溶菌酶、卵清蛋白、γ-球蛋白）的荧光猝灭表明，黄曲霉毒素对蛋白质不存在严格的特异性。
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