Affinity Chromatographic Quantitation of Glycosylated Hemoglobin in Newborn Infants
- 1 January 1983
- journal article
- research article
- Published by Taylor & Francis in Hemoglobin
- Vol. 7 (5) , 449-460
- https://doi.org/10.3109/03630268309038414
Abstract
Levels of glycosylated hemoglobin (glyco Hb) were determined in 45 newborn infants by affinity chromatography on phenylboro-nate-agarose gel and found to correlate well with the results obtained by two chemical methods. However the percentages of Hb FIad˚ and Hb FIc determined by Bio-Rex 70 chromatography did not correlate with the glyco Hb values. The glyco Hb levels in the newborns were significantly lower than in the adults. Rechromatography of the glyco and nonglyco Hb fractions on Bio-Rex 70 columns indicated that Hb F -like glyco Hb (presumably formed by glycosylation of the α chain amino terminus and e-amino groups of lysyl amino acids) constituted about 60% of the glyco Hb fraction, whereas both Hb FIc and Hb FOad˚ components contained only small portions of the glyco Hb.This publication has 19 references indexed in Scilit:
- Chemical quantitation of hemoglobin glycosylation: Fluorometric detection of formaldehyde released upon periodate oxidation of glycoglobinAnalytical Biochemistry, 1981
- Preparation and Use of a Boronic Acid Affinity Support for Separation and Quantitation of Glycosylated HemoglobinsAnalytical Letters, 1981
- Glycosylated minor components of human fetal hemoglobinBiochimica et Biophysica Acta (BBA) - Protein Structure, 1980
- On the chromatographic heterogeneity of human fetal hemoglobinBiochimica et Biophysica Acta (BBA) - Protein Structure, 1979
- The Glycosylation of Hemoglobin: Relevance to Diabetes MellitusScience, 1978
- Human Fetal Hemoglobin F1Published by Elsevier ,1971
- Life-span of the fetal red blood cellThe Journal of Pediatrics, 1967
- Chromatography of human hemoglobinJournal of Chromatography A, 1963
- Hemoglobin FI, an acetyl-containing hemoglobinBiochimica et Biophysica Acta, 1962
- The Relation between the Minor Components of Whole Normal Human Adult Hemoglobin as Isolated by Chromatography and Starch Block ElectrophoresisJournal of the American Chemical Society, 1961