Recombinant avidin and avidin-fusion proteins

被引:29
作者
Airenne, KJ [1 ]
Marjomäki, VS [1 ]
Kulomaa, MS [1 ]
机构
[1] Univ Jyvaskyla, Dept Biol & Environm Sci, FIN-40351 Jyvaskyla, Finland
来源
BIOMOLECULAR ENGINEERING | 1999年 / 16卷 / 1-4期
关键词
recombinant avidin; avidin-biotin; avidin fusion protein; baculovirus expression vector system; BEVS; affinity tag/handle; Semliki Forest virus; SFV; review;
D O I
10.1016/S1050-3862(99)00037-6
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
Both chicken egg-white avidin and its bacterial relative streptavidin are well known for their extraordinary high affinity with biotin (K-d similar to 10(-15) M). They are widely used as tools in a number of affinity-based separations, in diagnostic assays and in a variety of other applications. These methods have collectively become known as (strept)avidin-biotin technology. Biotin can easily and effectively be attached to different molecules, termed binders and probes, without destroying their biological activity. The exceptional stability of the avidin-biotin complex and the wide range of commercially available reagents explain the popularity of this system. In order by genetic engineering to modify the unwanted properties of avidin and to further expand the existing avidin-biotin technology, production systems for recombinant avidin and avidin-fusion proteins have been established. This review article presents an overview of the current status of these systems. Future trends in the production and applications of recombinant avidin and avidin-fusion proteins are also discussed. (C) 1999 Elsevier Science B.V. All rights reserved.
引用
收藏
页码:87 / 92
页数:6
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