Hemoglobin Hotel-Dieu β599 ASP → GLY (Gl). A New Abnormal Hemoglobin with high Oxygen Affinity
- 1 January 1981
- journal article
- research article
- Published by Taylor & Francis in Hemoglobin
- Vol. 5 (1) , 19-31
- https://doi.org/10.3109/03630268108996908
Abstract
Hemoglobin Hotel-Dieu was detected by isoelectric focusing during investigation of a patient who had erythrocytosis. This variant migrates on cellulose acetate electrophoresis to a cathodic position relative to Hb F. In hemoglobin Hotel-Dieu, aspartic acid is substituted by glycine in position 99 of the β chain. As in other abnormal hemoglobins in which substitution of this residue has occured, Hb Hotel-Dieu exhibits a high oxygen affinity and is associated with familial erythrocytosis.This publication has 13 references indexed in Scilit:
- Hemoglobin Bougardirey-Mali β119 (GH2) Gly → Val. An Electrophoretically Silent Variant Migrating in Isoelectrofocusing as Hb FHemoglobin, 1979
- Isoelectric focusing of human hemoglobin: its application to screening, to the characterization of 70 variants, and to the study of modified fractions of normal hemoglobinsBlood, 1978
- ISOELECTRIC-FOCUSING OF HUMAN HEMOGLOBIN - ITS APPLICATION TO SCREENING, TO CHARACTERIZATION OF 70 VARIANTS, AND TO STUDY OF MODIFIED FRACTIONS OF NORMAL HEMOGLOBINS1978
- Haemoglobin Radcliffe (α2β299(G1)Ala): A High Oxygen‐Affinity Variant Causing Familial PolycythaemiaBritish Journal of Haematology, 1977
- Hb Henri Mondor: β26 (B8) Glu → Val: A variant with a substitution localized at the same position as that of HbE β26 Glu → LysFEBS Letters, 1976
- Separation of Human Hemoglobins by Deae-Cellulose Chromatography using Glycine-Kcn-Nacl DevelopersHemoglobin, 1976
- Direct determination of 2,3-diphosphoglycerateAnalytical Biochemistry, 1970
- Hemoglobin Yakima: I. Clinical and Biochemical Studies*Journal of Clinical Investigation, 1967