Purification of chaperonins.

Journal Article · Fri Jan 01 04:00:00 UTC 1999 · Journal of Chromatography. B

DOI:https://doi.org/10.1016/S0378-4347(98)00503-9· OSTI ID:942322

Quaite-Randall, F; Joachimiak, A

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. Large 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 candidates. 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 different biological sources. The objective is to help new researchers obtain better quality samples of chaperonins from many new organisms.

• Research Organization: Argonne National Laboratory (ANL)
• Sponsoring Organization: USDOE
• DOE Contract Number: AC02-06CH11357
• OSTI ID: 942322
• Report Number(s): ANL/CMB/JA-30324
• Journal Information: Journal of Chromatography. B, Journal Name: Journal of Chromatography. B Journal Issue: 1999 Vol. 722; ISSN 1570-0232
• Country of Publication: United States
• Language: ENGLISH

Related Subjects

59 BASIC BIOLOGICAL SCIENCES
BIOLOGY
BIOTECHNOLOGY
CRYSTALLOGRAPHY
HEAT-SHOCK PROTEINS
HUMAN POPULATIONS
MEDICINE
NUCLEAR MAGNETIC RESONANCE
PROTEIN STRUCTURE
PROTEINS
PURIFICATION
REAGENTS