Inhibitory effect of superoxide dismutase on fructosamine assay.
- 1 January 1987
- journal article
- research article
- Published by Oxford University Press (OUP) in Clinical Chemistry
- Vol. 33 (1) , 147-149
- https://doi.org/10.1093/clinchem/33.1.147
Abstract
The fructosamine assay measures the degree of nonenzymatic protein glycation by virtue of the reducing properties of such proteins in alkaline conditions. We report the marked inhibitory effect of superoxide dismutase (EC 1.15.1.1) on the reducing activity both of protein glycated in vitro and of diabetic sera, indicating superoxide intermediacy in the fructosamine reaction. The free-radical intermediates may be of analytical significance when pathological and physiological changes in serum anti-oxidant activity occur. They may also be of pathological significance in diabetic microangiopathy and protein browning.This publication has 3 references indexed in Scilit:
- Self-perpetuating mechanisms of immunoglobulin G aggregation in rheumatoid inflammation.Journal of Clinical Investigation, 1985
- Non-enzymatically glycosylated serum protein in diabetes mellitus: An index of short-term glycaemiaDiabetologia, 1981
- Antioxidative Effect of Maillard Reaction IntermediatesPublished by Springer Nature ,1980