Abstract: Horse muscle acylphosphatase consists of a main chain S-S bound to glutathione. It was found that removal of the glutathione by reduction and successive carboxymethylation of the only cysteine of the main chain affects the stability of the enzyme, mainly with respect to thermal inactivation. On the other hand, the kinetic properties of the enzyme are affected very little.
Stability and kinetic behavior of carboxymethylated horse muscle acylphosphatase / M. Stefani; A. Berti; G. Camici; G. Manao; G. Cappugi; G. Ramponi. - In: PHYSIOLOGICAL CHEMISTRY AND PHYSICS. - ISSN 0031-9325. - STAMPA. - 10:(1978), pp. 367-373.
Stability and kinetic behavior of carboxymethylated horse muscle acylphosphatase
STEFANI, MASSIMO;BERTI, ANDREA;CAMICI, GUIDO;MANAO, GIAMPAOLO;CAPPUGI, GIANNI;RAMPONI, GIAMPIETRO
1978
Abstract
Abstract: Horse muscle acylphosphatase consists of a main chain S-S bound to glutathione. It was found that removal of the glutathione by reduction and successive carboxymethylation of the only cysteine of the main chain affects the stability of the enzyme, mainly with respect to thermal inactivation. On the other hand, the kinetic properties of the enzyme are affected very little.
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