The influence of glycation on the peroxidase activity of haemoglobin

Eur J Clin Chem Clin Biochem. 1994 Jun;32(6):435-40. doi: 10.1515/cclm.1994.32.6.435.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Aminosalicylic Acids / metabolism
  • Glycated Hemoglobin / metabolism*
  • Glycosylation
  • Humans
  • Hydrogen Peroxide / metabolism
  • Hydrogen-Ion Concentration
  • Mesalamine
  • Oxidation-Reduction
  • Peroxidase / metabolism*
  • Sorbitol / pharmacology

Substances

  • Aminosalicylic Acids
  • Glycated Hemoglobin A
  • Mesalamine
  • Sorbitol
  • Hydrogen Peroxide
  • Peroxidase