Rojo F, Ayala J A, de la Rosa E J, de Pedro M A, Arán V, Berenguer J, Vázquez D
J Antibiot (Tokyo). 1984 Apr;37(4):389-93. doi: 10.7164/antibiotics.37.389.
125I-Labeled derivatives of the beta-lactam antibiotics cephalexin, cephradine, cefaclor and 6-alpha-aminopenicillanic acid have been obtained by reacting these compounds with (125I)-Bolton-Hunter reagent. The following target proteins were found in Escherichia coli: (1) The derivatives of cephalexin, cefaclor and cephradine preferentially interact with the high molecular weight penicillin binding proteins ( PBP1a and PBP1b ); (2) The 125I- derivative of 6-alpha-aminopenicillanic acid is preferentially bound by the low molecular weight penicillin binding proteins 4 and 5/6. The iodinated derivatives showed a very high affinity of binding to their target proteins with apparent half-saturating concentrations in the nano -molar range.
通过使β-内酰胺抗生素头孢氨苄、头孢拉定、头孢克洛和6-α-氨基青霉烷酸与（125I）-博尔顿-亨特试剂反应，已获得了它们的125I标记衍生物。在大肠杆菌中发现了以下靶蛋白：（1）头孢氨苄、头孢克洛和头孢拉定的衍生物优先与高分子量青霉素结合蛋白（PBP1a和PBP1b）相互作用；（2）6-α-氨基青霉烷酸的125I衍生物优先与低分子量青霉素结合蛋白4和5/6结合。碘化衍生物显示出与它们的靶蛋白具有非常高的结合亲和力，表观半饱和浓度在纳摩尔范围内。
