PMID: 2310749Mar 1, 1990

The unfolding and attempted refolding of citrate synthase from pig heart

Biochimica Et Biophysica Acta
S M WestN C Price

Abstract

The unfolding of the dimeric enzyme citrate synthase from pig heart in solutions of guanidinium chloride (GdnHCl) was studied. Data from fluorescence, circular dichroism (CD) and thiol group reactivity studies indicated that the enzyme was almost completely unfolded at GdnHCl concentrations greater than or equal to 4 M. On dilution of GdnHCl, essentially no reactivation of the enzyme occurred. The implications of this finding for the process of folding and assembly in vivo of this and other mitochondrial enzymes are discussed. Exposure of the enzyme to high pH (9-10) led to only a small loss of secondary structure and partial reactivation could be observed on readjustment of the pH to 8.0.

References

Aug 1, 1989·Trends in Biochemical Sciences·R J Ellis, S M Hemmingsen
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Jan 1, 1986·Annual Review of Biophysics and Biophysical Chemistry·G Wiegand, S Remington
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Citations

Apr 1, 1992·Protein Science : a Publication of the Protein Society·W ZhiP A Srere
Jun 1, 1999·Science in China. Series C, Life Sciences·H ZhangZ Lin
Apr 1, 1992·The International Journal of Biochemistry·S M Kelly, N C Price
Jun 27, 2012·The Journal of Biological Chemistry·Magdalena BartoszewskaIda J van der Klei
May 25, 1999·Protein Science : a Publication of the Protein Society·A Ayed, H W Duckworth
May 29, 1998·Biochimica Et Biophysica Acta·B VenkateshaH S Savithri
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Dec 18, 2001·Journal of Molecular Biology·R MaierF X Schmid
Nov 13, 1999·Nature Cell Biology·B C BraunM Schmidt

Related Concepts

Metazoa
Circular Dichroism, Vibrational
Citrate (si)-Synthase
Enzyme Activation
Enzyme Reactivators
Guanidines
Hydrogen-Ion Concentration
Oxo-Acid-Lyases
Myocardium
Protein Conformation

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