Rothwell J T, Lacey E, Sangster N C
Elanco Animal Health, 16 Giffnock Ave, NSW 2113, Macquarie Park, Australia.
Int J Parasitol. 2000 May;30(6):769-75. doi: 10.1016/s0020-7519(00)00048-5.
Closantel binds to the serum proteins of the host and affects blood sucking parasites when they ingest the blood of treated hosts. Closantel binds specifically to ovine serum albumin (K(a) of 9. 3x10(6)M(-1)) at site I, the warfarin/phenylbutazone binding site of albumin Closantel also binds to invertebrate haemocyanin and haemolymph. The strongest binding of closantel in homogenates of H. contortus is found in fractions containing soluble proteins. This binding is of low affinity and, because the site itself is not fully denaturable, it may not be proteinaceous. There is no detectable difference in binding affinity between homogenate fractions from closantel susceptible and resistant isolates of adult or larval worms suggesting that closantel resistance is not due to changes in the closantel receptor or carrier.
氯氰碘柳胺与宿主血清蛋白结合，并在吸血寄生虫摄取经治疗宿主的血液时对其产生影响。氯氰碘柳胺在部位I特异性结合绵羊血清白蛋白（解离常数K(a)为9.3×10⁶M⁻¹），该部位是白蛋白的华法林/保泰松结合位点。氯氰碘柳胺还与无脊椎动物血蓝蛋白和血淋巴结合。在捻转血矛线虫匀浆中，氯氰碘柳胺的最强结合出现在含有可溶性蛋白的组分中。这种结合亲和力较低，并且由于该位点本身不能完全变性，所以它可能不是蛋白质性质的。在氯氰碘柳胺敏感和抗性的成虫或幼虫分离株的匀浆组分之间，未检测到结合亲和力的差异，这表明氯氰碘柳胺抗性并非由于氯氰碘柳胺受体或载体的变化所致。
