The heparin-binding site of human xanthine oxidase.
The enzyme xanthine oxidase (XOD) has an affinity for heparin and can bind to cultured porcine aortic endothelial cells. We have reported that the exposure of human XOD (h-XOD) to the lysine-specific reagent trinitrobenzenesulfonic acid or the arginine-specific reagent phenylglyoxal caused it to lose its affinity for heparin-Sepharose. The heparin-binding sites in h-XOD are further studied in the present article. From a chymotryptic digest of cyanogen bromide fragmented h-XOD, two peptides with an affinity for heparin-HPLC, A-1 and A-2, were isolated. Amino acid sequence analysis showed that both peptides had lysine and/or arginine residues. The A-1 region may direct its charged side chains toward the solvent while burying its hydrophobic side chains against the hydrophobic inside, because the A-1 peptide forms a highly amphipathic structure. Peptide A-2 contains triple lysine residues and constitutes a hydrophilic region.
Fukushima
T
T
Department of Pharmaceutics, Gifu Pharmaceutical University, Japan.
Adachi
T
T
Hirano
K
K
D000595:Amino Acid Sequence; D001665:Binding Sites; D002851:Chromatography, High Pressure Liquid; D002918:Chymotrypsin; D003488:Cyanogen Bromide; D006493:Heparin / Q000378:metabolism*; D006801:Humans; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry / Q000302:isolation & purification; D014969:Xanthine Oxidase / Q000378:metabolism*
D010455:Peptides; D006493:Heparin; D014969:Xanthine Oxidase; D002918:Chymotrypsin; D003488:Cyanogen Bromide