title: Adrenoferredoxin-binding peptide of NADPH-adrenoferredoxin reductase.
abstract: The amino-acid sequence at the adrenoferredoxin-binding site of NADPH-adrenoferredoxin reductase ferredoxin:NADP+ oxidoreductase, EC 1.18.1.2) from bovine adrenocortical mitochondria was investigated chemically. NADPH-adrenoferredoxin reductase has an essential lysine residue at the adrenoferredoxin-binding site. A polypeptide at the adrenoferredoxin-binding site was isolated by high-pressure liquid chromatography from NADPH-adrenoferredoxin reductase modified with pyridoxal 5'-phosphate and cleaved with cyanogen bromide. The amino-acid sequence of the adrenoferredoxin-binding peptide was identified. The peptide accounted for 95% of the sugar content of the NADPH-adrenoferredoxin reductase.
authors: Department of Biochemistry, Kagawa Medical School, Japan.
authors: I
authors: I
authors: Hamamoto
authors: K
authors: K
authors: Kurokohchi
authors: S
authors: S
authors: Tanaka
authors: Y
authors: Y
authors: Ichikawa
mesh_terms: D000302:Adrenal Cortex / Q000201:enzymology*; D000325:Adrenodoxin / Q000378:metabolism*; D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001665:Binding Sites; D002241:Carbohydrates / Q000032:analysis; D002417:Cattle; D002851:Chromatography, High Pressure Liquid; D003488:Cyanogen Bromide; D004591:Electrophoresis, Polyacrylamide Gel; D005287:Ferredoxin-NADP Reductase / Q000032:analysis / Q000378:metabolism*; D008928:Mitochondria / Q000201:enzymology; D008969:Molecular Sequence Data; D008970:Molecular Weight; D009247:NADH, NADPH Oxidoreductases / Q000378:metabolism*; D010446:Peptide Fragments / Q000302:isolation & purification / Q000378:metabolism*; D011732:Pyridoxal Phosphate
chemical_list: D000596:Amino Acids; D002241:Carbohydrates; D010446:Peptide Fragments; D000325:Adrenodoxin; D011732:Pyridoxal Phosphate; D005287:Ferredoxin-NADP Reductase; D009247:NADH, NADPH Oxidoreductases; D003488:Cyanogen Bromide