METAL-BINDING CHIMERIC ANTIBODIES EXPRESSED IN ESCHERICHIA-COLI

被引：14
|
作者：
SAWYER, JR [1 ]
TUCKER, PW [1 ]
BLATTNER, FR [1 ]
机构：
[1] UNIV TEXAS,SW MED CTR,DEPT MICROBIOL,DALLAS,TX 75235
来源：
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 1992年 / 89卷 / 20期
关键词：
RECOMBINANT ANTIBODIES; CANCER RADIOTHERAPY AND DIAGNOSTIC IMAGING; METALLOPROTEINS;
D O I：
10.1073/pnas.89.20.9754
中图分类号：
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号：
07 ; 0710 ; 09 ;
摘要：
Metallothionein, a well-characterized biological chelator of metals, has been genetically fused to the binding domain of an antibody and expressed in the periplasm of Escherichia coli. Specific delivery of Cd-109 to immobilized hapten or to haptenated cells was demonstrated directly in periplasmic extracts. This approach is potentially useful for targeted radiotherapy and diagnostic imaging. We find six to seven atoms of metal per active antigen-combining site. Absence of the Fc portion of the immunoglobulin along with low immunogenicity of metallothionein-metal complexes should reduce immunologic reactions.
引用
收藏
页码：9754 / 9758
页数：5
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