Fry M, Plummer D T
Chem Biol Interact. 1979 Apr;25(1):113-24. doi: 10.1016/0009-2797(79)90073-5.
The antibiotic cephaloridine has been shown to interact with phospholipid structures, using the techniques of ultraviolet difference spectroscopy, surface pressure measurements and liposome models. The results indicate that this interaction is at least partly hydrophobic in nature and help explain the disruptive effects of high concentrations of cephaloridine on both artificial and natural phospholipid structures (lysosomes). Low concentrations of cephaloridine were shown to inhibit a lysosomal membrane-bound phospholipase 2 and it is suggested that such an inhibition may explain the cephaloridine-induced stabilization of rat-kidney lysosomes.
运用紫外差光谱法、表面压力测量法和脂质体模型技术,已证实抗生素头孢菌素与磷脂结构存在相互作用。结果表明,这种相互作用本质上至少部分是疏水的,这有助于解释高浓度头孢菌素对人工和天然磷脂结构(溶酶体)的破坏作用。低浓度的头孢菌素被证明可抑制溶酶体膜结合的磷脂酶2,有人认为这种抑制作用可能解释了头孢菌素诱导的大鼠肾脏溶酶体的稳定。