title: The influence of glycation on the peroxidase activity of haemoglobin.
abstract: The peroxidase activity of haemoglobin A was characterized for non-glycated and glycated haemoglobin (HbA1) within the pH range 4.5 to 6.0, by measuring the rate of oxidation of 5-aminosalicylic acid following the degradation of H2O2. Glycation was found to significantly lower the pH activity of haemoglobin peroxidase throughout the pH range. However, in the presence of 100 mmol/l sorbitol the pH activity profile of glycated haemoglobin was significantly elevated whilst that of non-glycated haemoglobin remained unchanged.
authors.affiliation: Department of Clinical Biochemistry, London Hospital Medical College, U.K.
authors.forename: U Y
authors.initials: UY
authors.lastname: Khoo
authors.forename: D J
authors.initials: DJ
authors.lastname: Newman
authors.forename: W K
authors.initials: WK
authors.lastname: Miller
authors.forename: C P
authors.initials: CP
authors.lastname: Price
mesh_terms: D000636:Aminosalicylic Acids / Q000378:metabolism; D006442:Glycated Hemoglobin / Q000378:metabolism*; D006031:Glycosylation; D006801:Humans; D006861:Hydrogen Peroxide / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D019804:Mesalamine; D010084:Oxidation-Reduction; D009195:Peroxidase / Q000378:metabolism*; D013012:Sorbitol / Q000494:pharmacology
chemical_list: D000636:Aminosalicylic Acids; D006442:Glycated Hemoglobin; D006861:Hydrogen Peroxide; D019804:Mesalamine; D009195:Peroxidase; D013012:Sorbitol