Dec 15, 1975

The oxygen affinity of haemoglobin Tak, a variant with an elongated beta chain

Biochimica Et Biophysica Acta
K Imai, H Lehmann


The oxygen affinity was investigated of purified Hb Tak, a human haemoglobin variant with elongated beta-chains. A very low P50 value was found which was not influenced by the addition of 2,3 diphosphoglycerate. The n value was 1, indicating non-cooperativity. The oxygen equilibrium curve of the whole blood haemolysate containing Hbs A and Tak was close to that of Hb A at the top of the curve, while the bottom of the curve greatly deviated from the latter, indicative of small if any interaction between Hb A and Tak during oxygenation.

Mentioned in this Paper

Alveolar Ventilation Function
Whole Blood
Hemoglobin Subunit Beta
Plasma Protein Binding Capacity
Peptide Fragments
Diphosphoglyceric Acids
Hemoglobin Tak
Abnormal Hemoglobins

About this Paper

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