Fang S C, Lindstrom F T
J Pharmacokinet Biopharm. 1980 Dec;8(6):583-97. doi: 10.1007/BF01060055.
The acidic compounds, such as phenoxyacetic acids, substituted benzoic acids, or acetylsalicylic acid, were found to bind to bovine serum albumin (BSA). Among phenoxyacetic acids, the binding affinity to BSA was highest for 2,4,5-trichlorophenoxyacetic acid (2,4,5-T), which was approximately 4-, 24-, and 160-fold greater than those for 2,4-dichlorophenoxyacetic acid (2,4-D), o-chlorophenoxyacetic acid (CPA), and phenoxyacetic acid (PAA), respectively. There were two bound to serum albumins of other mammalian species. The binding affinity varied among species and also depended on the chemicals. However, the order of binding affinity in the albumin of each species remained the same as observed in BSA with few exceptions. Blood/tissue ratios of 14C from rats dosed with these 14C-labeled acids were highly correlated with the logarithm of the binding affinity constantsaffinity constants.
已发现酸性化合物，如苯氧乙酸、取代苯甲酸或乙酰水杨酸，能与牛血清白蛋白（BSA）结合。在苯氧乙酸中，2,4,5-三氯苯氧乙酸（2,4,5-T）与BSA的结合亲和力最高，分别比2,4-二氯苯氧乙酸（2,4-D）、邻氯苯氧乙酸（CPA）和苯氧乙酸（PAA）高约4倍、24倍和160倍。这些化合物与其他哺乳动物物种的血清白蛋白也有两种结合形式。结合亲和力因物种而异，也取决于化学物质。然而，除少数例外情况外，每种物种白蛋白中的结合亲和力顺序与在BSA中观察到的相同。用这些14C标记的酸给药的大鼠体内14C的血/组织比与结合亲和力常数的对数高度相关。
