Abstract
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.
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