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Aleksandra M. Rozhkova, Yuri A. Denisenko, Igor G. Sinelnikov, Ivan N. Zorov, Denis V. Erokhin, Vitaly G. Dzhavakhia
Application
of microbial recombinant protein MF3 in refolding
of plant chitinase
Abstract
Abstract. Expression of recombinant proteins is important for studying their
biological function. Most often, the expression system of the E. coli is
used for the primary description of protein properties. However, under
overexpression conditions, the rate of aggregation of target proteins often
exceeds the rate of proper folding, resulting in the formation of insoluble
inclusion bodies. Inclusion bodies are a clear disadvantage of the E. coli
expression system because they interfere with the release of target recombinant
proteins. One solution to the existing problem is the use of chaperone-like
proteins in vitro to refold the target protein. In this work, the recombinant
protein MF3 was taken as an example of a chaperone-like protein, which
increased the yield of soluble plant chitinase by 92% compared to the yield of
this protein using the standard refolding procedure.
Copyright (C) Chemistry Dept., Moscow State University, 2002
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