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羟基氯代芳香族化合物对人红细胞膜蛋白热致性质的影响

Thermotropic properties of human erythrocyte membrane proteins as affected by hydroxychloroaromatic compounds.

作者信息

Miller T L, Smith R J

出版信息

Arch Biochem Biophys. 1986 Oct;250(1):128-38. doi: 10.1016/0003-9861(86)90709-5.

DOI:10.1016/0003-9861(86)90709-5
PMID:3767368
Abstract

The thermal stability of the anion transport protein (band 3) and other proteins of the human erythrocyte membrane, as influenced by hydroxychloroaromatic (HO-Cl2-Ar) compounds, was studied by differential scanning calorimetry. Various hydroxychlorodiphenyl ethers (HO-Clx-DPEs) and hexachlorophene, but not pentachlorophenol, caused a marked decrease in the thermal stability of band 3. Most of the other calorimetric transitions of the erythrocyte membrane were only slightly affected. The activity of HO-Clx-DPEs toward lowering the transition temperature of band 3 generally increased with the degree of chlorination, and was somewhat dependent on the position of hydroxyl substitution. At higher concentrations of HO-Clx-DPEs, there was a decrease in the enthalpy change and a broadening of the endothermic transition of band 3. The order of effectiveness of these compounds, as determined from band 3 denaturation temperatures, was similar to the order of potency previously observed for hemolysis of human erythrocytes.

摘要

通过差示扫描量热法研究了羟基氯代芳烃(HO-Cl2-Ar)化合物对人红细胞膜阴离子转运蛋白(带3蛋白)及其他蛋白热稳定性的影响。各种羟基氯代二苯醚(HO-Clx-DPEs)和六氯酚(而非五氯酚)导致带3蛋白的热稳定性显著降低。红细胞膜的大多数其他量热转变仅受到轻微影响。HO-Clx-DPEs降低带3蛋白转变温度的活性通常随氯化程度的增加而增强,并且在一定程度上取决于羟基取代的位置。在较高浓度的HO-Clx-DPEs下,带3蛋白的焓变降低,吸热转变变宽。根据带3蛋白变性温度确定的这些化合物的有效性顺序,与先前观察到的人红细胞溶血效力顺序相似。

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Thermotropic properties of human erythrocyte membrane proteins as affected by hydroxychloroaromatic compounds.羟基氯代芳香族化合物对人红细胞膜蛋白热致性质的影响
Arch Biochem Biophys. 1986 Oct;250(1):128-38. doi: 10.1016/0003-9861(86)90709-5.
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