Literature DB >> 7918841

The influence of glycation on the peroxidase activity of haemoglobin.

U Y Khoo1, D J Newman, W K Miller, C P Price.   

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.

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Year:  1994        PMID: 7918841     DOI: 10.1515/cclm.1994.32.6.435

Source DB:  PubMed          Journal:  Eur J Clin Chem Clin Biochem        ISSN: 0939-4974


  4 in total

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2.  Experimental nonenzymatic glycosylation of vitreous collagens occurs by two pathways.

Authors:  J S Pulido
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3.  Non-enzymatic glycation induces structural modifications of myoglobin.

Authors:  Anjana Roy; Rajarshi Sil; Abhay Sankar Chakraborti
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4.  Effect of non-enzymatic glycation on esterase activities of hemoglobin and myoglobin.

Authors:  Subhrojit Sen; Tania Bose; Anjana Roy; Abhay Sankar Chakraborti
Journal:  Mol Cell Biochem       Date:  2007-02-14       Impact factor: 3.842

  4 in total

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