Removing Trace Fluorescent Contaminants from GroEL Preparations

Methods in Molecular Biology

Volumn 140, Issue , 2000, Pages 63-64

  Weber, Frank ^a  

^a MAX PLANCK INSTITUTE OF BIOCHEMISTRY   (Germany)

Author keywords

Excitation Wavelength; Fluorescence Measurement; Free Fraction; Native Condition; Peristaltic Pump

Indexed keywords

CHAPERONIN; COLORING AGENT; DYES, REAGENTS, INDICATORS, MARKERS AND BUFFERS; FLUORESCENT DYE; REACTIVE RED 120 DYE; TRIAZINE DERIVATIVE;

ARTICLE; CHEMISTRY; GEL CHROMATOGRAPHY; ION EXCHANGE CHROMATOGRAPHY; ISOLATION AND PURIFICATION; METHODOLOGY; PROTEIN DENATURATION; SPECTROFLUOROMETRY;

CHROMATOGRAPHY, GEL; CHROMATOGRAPHY, ION EXCHANGE; COLORING AGENTS; FLUORESCENT DYES; GROEL PROTEIN; INDICATORS AND REAGENTS; PROTEIN DENATURATION; SPECTROMETRY, FLUORESCENCE; TRIAZINES;

MLCS; MLOWN;

EID: 0034574712     PISSN: 10643745     EISSN: 19406029     Source Type: Book Series    
DOI: 10.1385/1-59259-061-6:63     Document Type: Chapter

References (6)

1. Lissin, N. M., Venyaminov, S., and Girshovich, A. S. (1990) (Mg-ATP)-depen-dent self-assembly of molecular chaperone GroEL. Nature 348, 339–342.
2. Ybarra, J. and Horowitz, P. M. (1995) Inactive GroEL monomers can be isolated and reassembled to functional tetradecamers that contain few bound peptides. J. Biol. Chem. 270, 22,962–22,967.
3. Ybarra, J. and Horowitz, P. M. (1995) Refolding and reassembly of active chaperonin GroEL after denaturation. J. Biol. Chem. 270, 22,113–22,115.
4. Weissman, J. S., Hohl, C. M., Kovalenko, O., Kashi, Y., Chen, S., Braig, K., et al. (1995) Mechanism of GroEL action: productive release of polypeptide from a sequestered position under GroES. Cell 83, 577–587.
5. Clark, A. C., Hugo, E., and Frieden, C. (1996) Determination of regions in the dihydrofolate reductase structure that interact with the molecular chaperonin GroEL. Biochemistry 35, 5893–5901.
6. Clark, A. C. and Frieden, C. (1997) GroEL-mediated folding of structurally homologous dihydrofolate reductases. J. Mol. Biol. 268, 512–525.