Both chicken egg-white avidin and its bacterial relative streptavidin are w
ell 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 se
parations, in diagnostic assays and in a variety of other applications. The
se methods have collectively become known as (strept)avidin-biotin technolo
gy. Biotin can easily and effectively be attached to different molecules, t
ermed binders and probes, without destroying their biological activity. The
exceptional stability of the avidin-biotin complex and the wide range of c
ommercially available reagents explain the popularity of this system. In or
der 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. T
his review article presents an overview of the current status of these syst
ems. 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.