BINDING OF I-125-LABELED B-LACTAM ANTIBIOTICS TO THE PENICILLIN BINDING-PROTEINS OF ESCHERICHIA-COLI

被引：12

作者：

ROJO, F ^{[1
]}

AYALA, JA ^{[1
]}

DELAROSA, EJ ^{[1
]}

DEPEDRO, MA ^{[1
]}

ARAN, V ^{[1
]}

BERENGUER, J ^{[1
]}

VAZQUEZ, D ^{[1
]}

机构：

[1] UNIV AUTONOMA MADRID, FAC CIENCIAS, CSIC, CTR BIOL MOLEC, MADRID 34, SPAIN

来源：

JOURNAL OF ANTIBIOTICS | 1984年 / 37卷 / 04期

关键词：

D O I：

10.7164/antibiotics.37.389

中图分类号：

Q81 [生物工程学（生物技术）]; Q93 [微生物学];

学科分类号：

071005 ; 0836 ; 090102 ; 100705 ;

摘要：

125I-Labeled derivatives of the .beta.-lactam antibiotics cephalexin, cephradine, cefaclor and 6-.alpha.-aminopenicillanic acid were obtained by reacting these compounds with (125I)-Bolton-Hunter reagent. Target proteins were found in Escherichia coli. The derivatives of cephalexin, cefaclor and cephradine preferentially interacted with the high MW penicillin binding proteins (PBP1a and PBP1b). The 125I-derivative of 6-.alpha.-aminopenicillanic acid was preferentially bound by the low MW 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.

引用

页码：389 / 393

页数：5

共 7 条

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