Purification of the plant alternative oxidase from Arum maculatum: measurement, stability and metal requirement
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 .
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
PLANT MITOCHONDRION
ALTERNATIVE OXIDASE
PROTEIN PURIFICATION
ENZYME ACTIVATION
QUINOL OXIDASE
DIIRON PROTEIN
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
PLANT MITOCHONDRION
ALTERNATIVE OXIDASE
PROTEIN PURIFICATION
ENZYME ACTIVATION
QUINOL OXIDASE
DIIRON PROTEIN