The availability of protein samples of sufficient quality and in sufficient
quantity is a driving force in biology and biotechnology. Protein samples
that are free of critical contaminants are required for specific assays, La
rge amounts of highly homogeneous and reproducible material are needed for
crystallography and nuclear magnetic resonance studies of protein structure
. Protein-based therapeutic factors used in human medicine must not contain
any contaminants that might interfere with treatment. The roles played by
molecular chaperones in protein folding and in many cellular processes make
these proteins very attractive candidates as biochemical reagents, and the
class of chaperones called chaperonins is one of the most important candid
ates. Methods for successfully purifying chaperonins are needed to advance
the field of chaperonin-mediated protein folding. This article outlines the
strategies and methods used to obtain pure chaperonin samples from differe
nt biological sources. The objective is to help new researchers obtain bett
er quality samples of chaperonins from many new organisms. (C) 1999 Publish
ed by Elsevier Science B.V.