TRYPSIN DISPLAY ON THE SURFACE OF BACTERIOPHAGE

被引:0
|
作者
COREY, DR
SHIAU, AK
YANG, Q
JANOWSKI, BA
CRAIK, CS
机构
[1] UNIV CALIF SAN FRANCISCO, DEPT PHARMACEUT CHEM, BOX 0446, SAN FRANCISCO, CA 94143 USA
[2] UNIV CALIF SAN FRANCISCO, DEPT BIOCHEM & BIOPHYS, SAN FRANCISCO, CA 94143 USA
关键词
ECOTIN; FUSION PROTEINS; PHAGE-M-13; PHAGEMID; PROTEIN ENGINEERING; SERINE PROTEASE;
D O I
暂无
中图分类号
Q3 [遗传学];
学科分类号
071007 ; 090102 ;
摘要
The gene III and VIII-encoded coat proteins (pIII and pVIII) from bacteriophage M13 have been fused to the C terminus of the serine protease, trypsin (Tsn). The genes encoding the fusions were then inserted directly into M 1 3mp 1 8 to create vectors which expressed both the Tsn-coat protein hybrids and the wild-type (wt) coat proteins. Immunoblot analysis confirmed that the bacteriophage express Tsn on their surface. Isolated fusion phage possess kinetic parameters which approximate those of the wt enzyme. An endogenous Escherichia coli protease inhibitor, ecotin, copurifies with the Tsn phage. Immobilized ecotin can be used to selectively bind bacteriophage which express Tsn=pIII fusion proteins.
引用
收藏
页码:129 / 134
页数:6
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