Further Characterization of Hb Henri Mondor or α2β226(B8)Glu→Val
- 1 January 1987
- journal article
- research article
- Published by Taylor & Francis in Hemoglobin
- Vol. 11 (1) , 1-11
- https://doi.org/10.3109/03630268709036574
Abstract
A second case of Hb Henri Mondor is reported. The subject, homozygous for Hb Henri Mondor, is of Algerian origin. The electro-phoretical behavior and structural characterization are given and discussed. Hb Henri Mondor, which is characterized by the replacement of the lysine residue in position β26, as is the case for Hb E, has normal functional properties and is normally expressed.This publication has 29 references indexed in Scilit:
- Abnormal processing of beta Knossos RNABlood, 1984
- Abnormal RNA processing due to the exon mutation of βE-globin geneNature, 1982
- Structural study of hemoglobin Knossos, β27 (B9) Ala→SerFEBS Letters, 1982
- Globin Chain Electrophoresis: a New Approach to the Determination of the Gγ/Aγ Ratio in Fetal Haemoglobin and to Studies of Globin SynthesisBritish Journal of Haematology, 1980
- 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
- Biosynthetic Ratio of Labelled Globin Chains in Human Reticulocytes, Determined by Electrophoresis on Cellulose AcetateHemoglobin, 1978
- 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
- Oxygen equilibrium of hemoglobin EJournal of Clinical Investigation, 1972
- A Simple Method for the Detection of Unstable HaemoglobinsBritish Journal of Haematology, 1972
- Estimation of Small Percentages of Fœtal HæmoglobinNature, 1959