The influence of glycation on the peroxidase activity of haemoglobin.
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.
Khoo
U Y
UY
Department of Clinical Biochemistry, London Hospital Medical College, U.K.
Newman
D J
DJ
Miller
W K
WK
Price
C P
CP
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
D000636:Aminosalicylic Acids; D006442:Glycated Hemoglobin; D006861:Hydrogen Peroxide; D019804:Mesalamine; D009195:Peroxidase; D013012:Sorbitol