Use of hydrostatic pressure to produce 'native' monomers of yeast enolase

European Journal of Biochemistry
M J KornblattClaude Balny

Abstract

The effects of hydrostatic pressure on yeast enolase have been studied in the presence of 1 mm Mn(2+). When compared with apo-enolase, and Mg-enolase, the Mn-enzyme differs from the others in three ways. Exposure to hydrostatic pressure does not inactivate the enzyme. If the experiments are performed in the presence of 1 mm Mg(2+), or with apo-enzyme, the enzyme is inactivated [Kornblatt, M.J., Lange R., Balny C. (1998) Eur. J. Biochem 251, 775-780]. The UV spectra of the high pressure forms of the Mg(2+)- and apo-forms of enolase are identical and distinct from the spectrum of the form obtained in the presence of 1 mm Mn(2+); this suggests that Mn(2+) remains bound to the high pressure form of enolase. With Mn-enolase, the various spectral changes do not occur in the same pressure range, indicating that multiple processes are occurring. Pressure experiments were performed as a function of [Mn(2+)] and [protein]. One of the changes in the UV spectra shows a dependence on protein concentration, indicating that enolase is dissociating into monomers. The small changes in the UV spectrum and the retention of activity lead to a model in which enolase, in the presence of high concentrations of Mn(2+), dissociates into native monomers...Continue Reading

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Citations

Nov 20, 2009·The Protein Journal·Dénison S Sánchez-MiguelClaudia G Benítez-Cardoza
Jun 14, 2005·Biochimica Et Biophysica Acta·Patrick Masson, Claude Balny
Apr 17, 2007·Journal of the American Society for Mass Spectrometry·Catherine S KaddisJoseph A Loo
Nov 9, 2005·Biochimica Et Biophysica Acta·Claude Balny
Aug 6, 2005·Brazilian Journal of Medical and Biological Research = Revista Brasileira De Pesquisas Médicas E Biológicas·S MarchalC Balny
Mar 15, 2005·Yeast
Apr 6, 2019·Protein and Peptide Letters·Cadena-Cadena FranciscoRivero-Espejel Ignacio Alfredo
Oct 31, 2014·Physical Chemistry Chemical Physics : PCCP·Eva KutálkováMarek Ingr

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