Preparation and some properties of a dimeric form (S-S) of horse muscle acylphosphatase.
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.
D017766:Acid Anhydride Hydrolases; D000818:Animals; D001205:Ascorbic Acid / Q000378:metabolism; D004220:Disulfides; D005612:Freeze Drying; D006736:Horses; D007700:Kinetics; D008970:Molecular Weight; D009132:Muscles / Q000201:enzymology; D010755:Organophosphates; D010084:Oxidation-Reduction; D010100:Oxygen / Q000378:metabolism; D010447:Peptide Hydrolases / Q000494:pharmacology; D010744:Phosphoric Monoester Hydrolases / Q000378:metabolism*; D011725:Pyridines / Q000378:metabolism; D013696:Temperature; D014508:Urea; D000097024:Acylphosphatase
D017766:Acid Anhydride Hydrolases; D001205:Ascorbic Acid; D004220:Disulfides; D010755:Organophosphates; D010100:Oxygen; D010447:Peptide Hydrolases; D010744:Phosphoric Monoester Hydrolases; D011725:Pyridines; D014508:Urea; D000097024:Acylphosphatase