Veronese F M, Bevilacqua R, Boccù E, Benassi C A
Farmaco Sci. 1977 Apr;32(4):303-10.
The binding of some cephalosporin antibiotics, namely cephalothin, cephaloridine and cephalexin, to serum albumins was quantitized using a fluorescence probe technique. The results suggest that these drugs bind to hydrophobic sites on serum albumins. The association constants of the three drugs with bovine serum albumin showed the strongest binding for cephalothin (Ka 1.2 x 10(3) M(1)) and weaker ones for cephaloridine and cephalexin (Ka 0.59 and 0.4 x 10(3) M(-1)). Serum albumin from different species was also investigated, only minor variations in the binding properties being found.
使用荧光探针技术对一些头孢菌素抗生素,即头孢噻吩、头孢噻啶和头孢氨苄与血清白蛋白的结合进行了定量分析。结果表明,这些药物与血清白蛋白上的疏水位点结合。这三种药物与牛血清白蛋白的缔合常数显示,头孢噻吩的结合力最强(Ka 1.2×10³ M⁻¹),而头孢噻啶和头孢氨苄的结合力较弱(Ka 0.59和0.4×10³ M⁻¹)。还研究了来自不同物种的血清白蛋白,发现结合特性仅有微小差异。