The structural feature surrounding glycated lysine residues in human hemoglobin
نویسندگان
چکیده
منابع مشابه
Glycated hemoglobin in fractionated erythrocytes.
Erythrocytes were fractionated, by centrifugation, on the basis of cell density, which is proportional to cell age. Glycated hemoglobin (Hb A1c) in the fractionated cells was measured and compared with the Hb A1c in whole blood and with the fructosamine concentrations in plasma of normal and diabetic subjects. In normal subjects, Hb A1c increased according to the age of the erythrocytes, but hy...
متن کاملGlycated Lysine Residues: A Marker for Non-Enzymatic Protein Glycation in Age-Related Diseases
Nonenzymatic glycosylation or glycation of macromolecules, especially proteins leading to their oxidation, play an important role in diseases. Glycation of proteins primarily results in the formation of an early stage and stable Amadori-lysine product which undergo further irreversible chemical reactions to form advanced glycation endproducts (AGEs). This review focuses these products in lysine...
متن کاملBiological variability of glycated hemoglobin.
BACKGROUND The measurement of glycated hemoglobin (HbA(1c)) has a pivotal role in monitoring glycemic state in diabetic patients. Furthermore, the American Diabetes Association has recently recommended the use of HbA(1c) for diabetes diagnosis, but a clear definition of the clinically allowable measurement error is still lacking. Information on biological variability of the analyte can be used ...
متن کاملPersistence of Individual Variations in Glycated Hemoglobin
OBJECTIVE To determine the individual persistence of the relationship between mean sensor glucose (MG) concentrations and hemoglobin A(1c) (A1C) from the Juvenile Diabetes Research Foundation Continuous Glucose Monitoring (CGM) Randomized Trial. RESEARCH DESIGN AND METHODS MG was calculated using CGM data for 3 months before A1C measurements at 3, 6, 9, and 12 months for the CGM group and at ...
متن کاملLysine residues involved in the active site
Egg-white avidin was treated with 1 -fluoro-2,4-dinitrobenzene. Modification of an average of one lysine residue per avidin subunit caused the complete loss of biotin binding. Tryptic peptides obtained from the 2,4-dinitrophenylated avidin were fractionated by reversed-phase h.p.l.c. Three peptides contained the 2,4-dinitrophenyl group. Amino acid analysis revealed that lysine residues 45, 94 a...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Biomedical Research
سال: 2011
ISSN: 1880-313X,0388-6107
DOI: 10.2220/biomedres.32.217