Increase in the glucosylated form of erythrocyte Cu-Zn-superoxide dismutase in diabetes and close association of the nonenzymatic glucosylation with the enzyme activity

• Published in: Biochimica et biophysica acta Vol. 924; no. 2; pp. 292 - 296
• Main Authors: Arai, Katsura, Iizuka, Susumu, Tada, Yoshihiko, Oikawa, Kiyoshi, Taniguchi, Naoyuki
• Format: Journal Article
• Language: English
• Published: Amsterdam Elsevier B.V 19.05.1987; Elsevier; North-Holland
• Subjects: Analytical, structural and metabolic biochemistry; Biological and medical sciences; Blood Glucose - metabolism; Copper; Diabetes; Diabetes Mellitus - enzymology; Enzymes and enzyme inhibitors; Erythrocytes - enzymology; Fundamental and applied biological sciences. Psychology; Glucosylation; Glycosylation; Human eruthrocyte; Humans; Oxidoreductases; Protein Processing, Post-Translational; Structure-Activity Relationship; Superoxide dismutase; Superoxide Dismutase - blood; Zinc; Superoxide dismutase; Glucosylation; Diabetes; Human eruthrocyte; Human; Purification; Enzyme; Red blood cell; Copper; Zinc
• ISSN: 0304-4165; 0006-3002; 1872-8006
• DOI: 10.1016/0304-4165(87)90025-0

Human erythrocytes contain glucosylated and nonglucosylated CuZnsuperoxide dismutases which can be separated by boronate affinity chromatography. The percentage of the glucosylated form is significantly increased in the erythrocytes of patients with diabetes as compared to normal erythrocytes. The...