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Degradation of glycated hemoglobin role of erythrocytic proteolytic enzymes and oxidant damage

Chaerkadi, Raghothama and Rao, Pragna (1997) Degradation of glycated hemoglobin role of erythrocytic proteolytic enzymes and oxidant damage. Clinica chimica acta, 264 (1). pp. 13-25.

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Abstract

Glycated hemoglobin can be degraded by proteolytic enzyme(s) in the erythrocyte. The enzyme(s) co-elutes with glycated hemoglobin when the latter is separated from erythrocyte lysates using the cation-exchanger Bio Rex-70. A further purification of the Bio Rex eluant on DEAE Sephadex A-50 separated the enzyme(s) from glycated hemoglobin. Studies with the Bio Rex eluant showed that degradation of glycated hemoglobin is maximum at 37 degrees C at pH 8.6. Proteolytic degradation is inhibited by 5 mM N-ethylmaleimide (NEM), 5 mM ethylenediamine tetraacetic acid (EDTA) and 0.6 mM n-p-tosyl-L-lysine choromethyl ketone (TLCK) (100-87 and 76% inhibition respectively). This study also examines the possibility that oxidative-damage to glycated hemoglobin increases its susceptibility to proteolytic degradation. When incubated with various anti-oxidants like DTPA, uric acid, mannitol and butylated hydroxy toluene (BHT), proteolytic degradation of glycated hemoglobin decreased by 66.1, 50.7 and 38% respectively

Item Type: Article
Uncontrolled Keywords: Glycated hemoglobin ; Oxidant damaged hemoglobin ; Erythrocytes ; Proteolytic enzymes ; Diabetes mellitus
Subjects: Medicine > KMC Manipal > Biochemistry
Depositing User: KMC Manipal
Date Deposited: 13 Jan 2012 10:02
Last Modified: 13 Jan 2012 10:02
URI: http://eprints.manipal.edu/id/eprint/2480

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