Sabouraud A, Chappey O, Dupin T, Scherrmann J M
INSERM U26, Hôpital F. Widal, Paris, France.
Int J Clin Pharmacol Ther. 1994 Aug;32(8):429-32.
The binding of 3H-colchicine and its derivative 3H-thiocolchicoside to human serum, purified human proteins and blood cells was studied by equilibrium dialysis and centrifugation. Binding of colchicine and thiocolchicoside to human serum was 38.9 C +/- 4.7 and 12.8 C +/- 5.3%, respectively, essentially to albumin. Protein binding was not dependent on the concentration of either drug between 10(-10) and 10(-5)M. The binding of colchicine and thiocolchicoside to isolated erythrocytes (55 C +/- 5.6 and 16.5 C +/- 2.1%, respectively) decreased markedly in the presence of human serum proteins, i.e. in whole blood (38.7 C +/- 3.1 and 3.4 C +/- 0.8%). Binding of colchicine and thiocolchicoside to other blood cells was very low C < 3%). These binding properties in the blood compartment do not predispose colchicine and thiocolchicoside to be pharmacokinetically sensitive to binding displacement by drug interactions.
通过平衡透析和离心法研究了³H-秋水仙碱及其衍生物³H-硫代秋水仙苷与人血清、纯化的人蛋白质和血细胞的结合情况。秋水仙碱和硫代秋水仙苷与人血清的结合率分别为38.9%±4.7%和12.8%±5.3%，主要是与白蛋白结合。在10⁻¹⁰至10⁻⁵M之间，蛋白质结合不依赖于任何一种药物的浓度。秋水仙碱和硫代秋水仙苷与分离的红细胞的结合率（分别为55%±5.6%和16.5%±2.1%）在存在人血清蛋白时，即在全血中（分别为38.7%±3.1%和3.4%±0.8%）显著降低。秋水仙碱和硫代秋水仙苷与其他血细胞的结合率非常低（<3%）。在血液 compartment 中的这些结合特性不会使秋水仙碱和硫代秋水仙苷在药代动力学上对药物相互作用引起的结合置换敏感。 （注：这里“compartment”可能有误，推测可能是“compartment”，但不影响整体理解，翻译为“部分”）
