Zhou X H, van der Helm D, Venkatramani L
Department of Chemistry and Biochemistry, University of Oklahoma, Norman, USA.
Biometals. 1995 Apr;8(2):129-36. doi: 10.1007/BF00142012.
The dissociation constants for the binding of ferric enterobactin with FepA and FecA are quantitated with displacement experiments. It is found that Kd for FepA is 12 times lower than the one for FecA. This indicates that FepA is an high-affinity receptor while FecA binds ferric enterobactin with a lower affinity. Monoclonal antibodies specific for binding epitopes of FepA inhibit the binding of ferric enterobactin with purified FepA. These same antibodies do not inhibit the binding of ferric enterobactin with purified FecA. This indicates that the binding epitopes in FecA and FepA are different.
通过置换实验对铁肠杆菌素与FepA和FecA结合的解离常数进行了定量测定。结果发现，FepA的解离常数Kd比FecA的低12倍。这表明FepA是一种高亲和力受体，而FecA与铁肠杆菌素的结合亲和力较低。针对FepA结合表位的单克隆抗体可抑制铁肠杆菌素与纯化的FepA的结合。同样这些抗体不会抑制铁肠杆菌素与纯化的FecA的结合。这表明FecA和FepA中的结合表位不同。
