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应用蛋白质修饰的方法,从分子水平对豚鼠肺内两种不同亲和性M受体结合部位的分子结合特性进行了研究。结果表明:这两种不同亲和性M受体结合部位在分子构象上存在着差异。在与配基结合时,高亲和性M受体结合部位依赖于受体蛋白质中巯基的存在,而低亲和性M受体结合部位则依赖于双硫键的存在。
The molecular binding characteristics of two different affinity M receptor binding sites in guinea pig lung were studied at the molecular level by protein modification. The results show that there are differences in molecular conformation between the two different affinity M receptor binding sites. Upon binding to the ligand, the high-affinity M receptor binding site relies on the presence of sulfhydryl groups in the receptor protein whereas the low-affinity M receptor binding site is dependent on the presence of the disulfide bond.