Abstract: The thermal stability of horse muscle acylphosphatase was investigated by measuring the inactivation constants at various pH and temperature values, and by differential spectra technique. This enzyme has high thermal stability in an acidic environment but is inactivated in an alkaline medium. It was found that the enzyme can be protected against such inactivation at pH 8.0 by increasing its concentration and the ionic strength of the solution. The effect of high urea concentrations on stability was also measured. It was found that spectral changes at 230 nm are related to urea inactivation of the enzyme, and that the enzymatic activity can be instantly and almost completely restored by dilution of the urea.
Stability of horse muscle acylphosphatase to heat and to urea / A. Berti; M. Stefani; G. Camici; G. Manao; G. Ramponi. - In: PHYSIOLOGICAL CHEMISTRY AND PHYSICS. - ISSN 0031-9325. - STAMPA. - 10:(1978), pp. 153-162.
Stability of horse muscle acylphosphatase to heat and to urea
BERTI, ANDREA;STEFANI, MASSIMO;CAMICI, GUIDO;MANAO, GIAMPAOLO;RAMPONI, GIAMPIETRO
1978
Abstract
Abstract: The thermal stability of horse muscle acylphosphatase was investigated by measuring the inactivation constants at various pH and temperature values, and by differential spectra technique. This enzyme has high thermal stability in an acidic environment but is inactivated in an alkaline medium. It was found that the enzyme can be protected against such inactivation at pH 8.0 by increasing its concentration and the ionic strength of the solution. The effect of high urea concentrations on stability was also measured. It was found that spectral changes at 230 nm are related to urea inactivation of the enzyme, and that the enzymatic activity can be instantly and almost completely restored by dilution of the urea.
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