Image from Google Jackets

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

Tipo de material: TextoTextoSeries ; Biochimica et Biophysica Acta (BBA)- Bioenergetics , 1608(2-3), p.181-189, 2004Trabajos contenidos:
  • Affourtit, C
  • Moore. A.L
Tema(s): Recursos en línea: Resumen: 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
Tags from this library: No tags from this library for this title. Log in to add tags.
Star ratings
    Average rating: 0.0 (0 votes)
Holdings
Item type Current library Collection Call number Status Date due Barcode
Documentos solicitados Documentos solicitados CICY Documento préstamo interbibliotecario Ref1 B-6890 (Browse shelf(Opens below)) Available

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

There are no comments on this title.

to post a comment.