Abstract: The use of sodium selenite as a catalyst in the presence of oxygen was a suitable technique to obtain in good yield an interchain S-S dimeric form of horse muscle acylphosphatase. The dimer so obtained possesses kinetic properties very similar to those of the native enzyme. On the other hand the dimer has shown a generally lower stability in respect of the thermal inactivation, particularly in the acidic environment, to the lyophilization and to the proteolytic attack. As regards the 8 M urea inactivation, the dimer is not able to completely regain its activity by dilution, showing a behaviour quite different from that of the native enzyme.
Preparation and some properties of a dimeric form (S-S) of horse muscle acylphosphatase / M. Stefani; A. Berti; G. Camici; G. Manao; G. Cappugi; G. Ramponi. - In: INTERNATIONAL JOURNAL OF PEPTIDE & PROTEIN RESEARCH. - ISSN 0367-8377. - STAMPA. - 14:(1979), pp. 227-233.
Preparation and some properties of a dimeric form (S-S) of horse muscle acylphosphatase
STEFANI, MASSIMO;BERTI, ANDREA;CAMICI, GUIDO;MANAO, GIAMPAOLO;CAPPUGI, GIANNI;RAMPONI, GIAMPIETRO
1979
Abstract
Abstract: The use of sodium selenite as a catalyst in the presence of oxygen was a suitable technique to obtain in good yield an interchain S-S dimeric form of horse muscle acylphosphatase. The dimer so obtained possesses kinetic properties very similar to those of the native enzyme. On the other hand the dimer has shown a generally lower stability in respect of the thermal inactivation, particularly in the acidic environment, to the lyophilization and to the proteolytic attack. As regards the 8 M urea inactivation, the dimer is not able to completely regain its activity by dilution, showing a behaviour quite different from that of the native enzyme.I documenti in FLORE sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.