Kinetics of glycosylated haemoglobin in uraemia determined on ion-exchange and affinity chromatography: no increase in the rate of glycosylation.
The haemoglobin glycosylation in uraemia was studied by determination of labile and stable HbA1 in patients and by kinetical experiments in vitro. The influence of uraemia on stable and labile HbA1 was investigated in a clinical study of 32 non-diabetic and 20 diabetic patients with uraemia compared with controls. Glycosylated haemoglobin (GHb) was determined with ion-exchange chromatography (IEC). A highly significant elevation of stable as well as labile HbA1 was found in uraemic non-diabetics and of stable HbA1 in uraemic diabetics. This elevation was not related to blood glucose level. Labile HbA1 does not significantly affect the increased total level of GHb. An in vitro study using IEC and affinity gel chromatography on erythrocytes sequentially incubated in glucose and saline showed identical kinetics of GHb formation and elimination in uraemic and in non-uraemic patients. No indication of changed glycosylation by the uraemia was found.
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Wettre
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Lundberg
D000328:Adult; D000368:Aged; D002846:Chromatography, Affinity / Q000379:methods; D002852:Chromatography, Ion Exchange / Q000379:methods; D006442:Glycated Hemoglobin / Q000378:metabolism*; D006801:Humans; D007700:Kinetics; D008875:Middle Aged; D014511:Uremia / Q000097:blood*
D006442:Glycated Hemoglobin