1. Hb Helsinki: a variant with a high oxygen affinity and a substitution at a 2,3-DPG binding site (beta82[EF6] Lys replaced by Met).
- Author
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Ikkala E, Koskela J, Pikkarainen P, Rahiala EL, El-Hazmi MA, Nagai K, Lang A, and Lehmann H
- Subjects
- Adult, Aged, Amino Acids analysis, Binding Sites, Electrophoresis, Paper, Electrophoresis, Starch Gel, Female, Humans, Male, Methionine blood, Middle Aged, Oxygen blood, Partial Pressure, Phytic Acid pharmacology, Polycythemia blood, Protein Binding, Diphosphoglyceric Acids blood, Hemoglobins, Abnormal analysis, Oxyhemoglobins analysis, Polycythemia genetics
- Abstract
A new haemoglobin, Hb Helsinki, in which beta 82-Lys (EF6) is replaced by Met, was found in a Finnish family. It was associated with familial erythrocytosis, and the oxygen affinity of the blood was higher than normal. The oxygen equilibrium curves of purified Hb Helsinki and HbA from the same haemolysate have been determined under vaious conditions. "Stripped' Hb Helsinki was found to show normal cooperativity, slightly low oxygen affinity and a reduced Bohr effect at physiological pH. However, the organic phosphates, 2,3-diphosphoglycerate (2,3-DPG) and inositol hexaphosphate (IHP) had a very small effect on Hb Helsinki, and the 2,3-DPG binding constant of deoxygenated Hb Helsinki is close to that of oxyhaemoglobin A. Thus, the replacement of Lys by Met at position 82 dramatically changes the nature of the central cavity of the tetramer and the effect of 2,3-DPG on the respiratory function of the molecule.
- Published
- 1976
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