Limited proteolysis of bovine adrenodoxin reductase: evidence for a domain structure.
Treatment of bovine adrenodoxin reductase with trypsin under conditions of limited proteolysis yields two major fragments of apparent molecular weights 30,500 and 20,200. The fragments, which have been partially purified by affinity chromatography to remove most of the intact adrenodoxin reductase, retain adrenodoxin-dependent NADPH cytochrome c reductase activity. Kinetic analyses yield Vmax and Km (adrenodoxin) values of 485 min-1 and 0.96 microM, respectively, at an ionic strength of 0.13 M in comparison to 1059 min-1 and 0.40 microM, respectively, for intact adrenodoxin reductase under the same conditions.
D000302:Adrenal Cortex / Q000201:enzymology; D000818:Animals; D002417:Cattle; D003488:Cyanogen Bromide; D005287:Ferredoxin-NADP Reductase / Q000378:metabolism*; D007700:Kinetics; D008970:Molecular Weight; D009247:NADH, NADPH Oxidoreductases / Q000378:metabolism*; D009251:NADPH-Ferrihemoprotein Reductase / Q000378:metabolism; D010446:Peptide Fragments / Q000378:metabolism; D014357:Trypsin
D010446:Peptide Fragments; D005287:Ferredoxin-NADP Reductase; D009247:NADH, NADPH Oxidoreductases; D009251:NADPH-Ferrihemoprotein Reductase; D014357:Trypsin; D003488:Cyanogen Bromide