Wu C, Mathews K P
Immunopharmacology. 1986 Aug;12(1):53-8. doi: 10.1016/0162-3109(86)90051-2.
Both nitroreductase and transglutaminase activities have been assayed in the 10,000 X g supernatant fluids of rat intestine homogenates after Triton X-100 treatment. Incubation of 14C-nitrofurantoin in the intestine extract yielded protein-bound 14C-labeled products. Injection into rabbits of the conjugated protein similarly prepared with unlabeled nitrofurantoin elicited formation of antibodies against nitrofurantoin. These results suggest that intestinal metabolism and conjugation to protein of orally administered drugs may serve as a probable mechanism of drug allergy, and this may be accomplished by enzymatic coupling of relatively stable drug metabolites to protein carriers.
在用Triton X-100处理后的大鼠肠道匀浆10000×g上清液中，已对硝基还原酶和转谷氨酰胺酶活性进行了测定。在肠道提取物中孵育14C-呋喃妥因可产生与蛋白质结合的14C标记产物。用未标记的呋喃妥因同样制备的结合蛋白注射到兔子体内，可引发抗呋喃妥因抗体的形成。这些结果表明，口服药物的肠道代谢及与蛋白质的结合可能是药物过敏的一种可能机制，这可能是通过相对稳定的药物代谢产物与蛋白质载体的酶促偶联来实现的。
