GENERATION OF STABLE DIMERS WITH REVERSIBLE BIOTIN-BINDING ACTIVITY

摘要

Avidin is mutated by replacing the Trp110 with Lys, and streptavidin is mutated by replacing the Trp120 with Lys. Both of these mutant proteins produce a stable dimer. These stable dimers exhibit reversible biotin-binding properties. The mutant avidin and streptavidin can be used in all known avidin/streptavidin-biotin systems and purification processes, with the added advantage that the avidin/streptavidin and biotin may be eventually separated.