Table II.

Relative activity of NADPH oxidase activity bands (103–106 and 75–80 kD) in the fractionated supernatant and membrane proteins in the SDS in-gel assay

FractionMolecularSoluble ProteinRelative ActivityTotal Relative Activity (Soluble Protein × Relative Activity)
kD μ fraction−1
Supernatant (203,000 g)103–106813,00000
77–8000
Pellet (203,000 g)103–1068,950435,800
77–80435,800
Lower phase103–1063501350
77–8031,050
Upper phase103–10637010037,000
77–80155,550
  • F2-a  Extracts from 150 g of tomato leaves were centrifuged at 10,000g. The supernatant was subjected to centrifugation at 203,000g to yield the microsomal fraction. Lower and upper phases were partitioned from the microsomal fraction by the two-phase system and fractionated by SDS-PAGE as described in “Materials and Methods.” The activity gels were scanned and the results presented in arbitrary relative units.