Purification of the plant alternative oxidase from Arum maculatum: measurement, stability and metal requirement 

 -  Biochimica et Biophysica Acta (BBA)- Bioenergetics , 1608(2-3), p.181-189, 2004 .
<br/><br/> We have purified plant alternative oxidase (AOX)protein from the spadices of thermogenic Arum maculatum (cuckoo pint)to virtual homogeneity. The obtained enzyme fraction exhibits a high specific activity, consuming on average 32 µmol oxygen min-1 mg-1, which is completely stable for at least 6 months when the sample is stored at -70 °C. This exceptionally stable AOX activity is inhibited approximately 90 
<br/><br/><label>Subjects--Topical Terms: </label><br/>PLANT MITOCHONDRION<br/>ALTERNATIVE OXIDASE<br/>PROTEIN PURIFICATION<br/>ENZYME ACTIVATION<br/>QUINOL OXIDASE<br/>DIIRON PROTEIN