Nonenzymatic glycation of immunoglobulins does not impair antigen-antibody binding.

Author:

Morin L G,Austin G E,Burkhalter A

Abstract

Abstract We glycated immunoglobulins from commercial kits designed to measure human ferritin, thyrotropin, and transferrin, and compared the calibration curves for assays utilizing glycated antibodies with those of assays utilizing non-glycated antibodies. Glycation was verified by borate affinity chromatography and assay with thiobarbituric acid reagent. We found no evidence that antigen-antibody binding is impaired by nonenzymatic glycation of antibodies. Our results provide no evidence in support of the supposition that glycation may be a contributory factor in the decreased resistance of diabetics to infection.

Publisher

Oxford University Press (OUP)

Subject

Biochemistry (medical),Clinical Biochemistry

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1. Protein glycation in diabetes mellitus;Advances in Clinical Chemistry;2023

2. Some views on proteomics in diabetes;Clinical Chemistry and Laboratory Medicine;2011-01-01

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4. Immunoglobulin glycation with fructose: A comparative study;Clinica Chimica Acta;2007-03

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