Elevation of the Hemoglobin Al Fraction in Alcoholism
- 1 March 1982
- journal article
- research article
- Published by Wiley in Alcohol, Clinical and Experimental Research
- Vol. 6 (2), 260-266
- https://doi.org/10.1111/j.1530-0277.1982.tb04972.x
Abstract
The proportion of Hb A1 was measured in 43 normoglycemic men and women admitted consecutively to an alcohol treatment center and in 41 healthy volunteers. On the average, the size of the fraction was significantly greater in the alcoholic patients than in the healthy subjects. The results of Hb A1c determinations added independent evidence that this difference was not due to formation of any of the known glycosylated Hb despite the fact that the alcohol-related Hb cochromatographed with Hb A1c. The size of the Hb A1 fraction was unrelated to the presence or absence of alcoholic hepatitis, although most patients having abnormally high serum hepatic enzyme activities also had abnormal elevations of the A1 fraction. Some patients with normal serum enzyme activities were among those having the highest values of the A1 fraction, indicating that the latter was a more sensitive indicator of excessive alcohol intake than were hepatic enzyme activities. The proportion Hb A1 in a patient followed over a period of 9 mo. rose to a maximum as the patient continued to drink. In a patient who abstained from drinking while under hospital care, the A1 fraction decreased towards normal with a half-time of 11 days. Alcohol-related Hb is apparently a product of a readily reversible reaction occurring at a maximal rate of 0.038 mM day-1, about 4 times as rapid as is the formation of Hb A1c.This publication has 21 references indexed in Scilit:
- Acetaldehyde adducts with hemoglobin.Journal of Clinical Investigation, 1981
- Acetaldehyde-Dependent Changes in Hemoglobin and Oxygen Affinity of Human ErythrocytesHemoglobin, 1981
- Heterogeneity and new molecular forms of human liver alcohol dehydrogenaseBiochemical and Biophysical Research Communications, 1979
- Adduct formation between hemoglobin and 5-deoxy-D-xylulose-1-phosphateBiochemical and Biophysical Research Communications, 1979
- Synthesis of 5-deoxy-D-xylulose-1-phosphate by human erythrocytesBiochemical and Biophysical Research Communications, 1979
- The biosynthesis of human hemoglobin A1c. Slow glycosylation of hemoglobin in vivo.Journal of Clinical Investigation, 1976
- Studies on the properties of the human alcohol dehydrogenase isozymes determined by the different loci ADH1, ADH2, ADH3Annals of Human Genetics, 1973
- The metabolism of deoxyribonucleoside by the human erythrocyteBiochimica et Biophysica Acta (BBA) - General Subjects, 1968
- 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
- Observations on the Chromatographic Heterogeneity of Normal Adult and Fetal Human Hemoglobin: A Study of the Effects of Crystallization and Chromatography on the Heterogeneity and Isoleucine ContentJournal of the American Chemical Society, 1958