@article {1172126, title = {The oxygen affinity of haemoglobin Tak, a variant with an elongated beta chain}, journal = {Biochim Biophys Acta}, volume = {412}, number = {2}, year = {1975}, month = {1975 Dec 15}, pages = {288-94}, abstract = {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.}, keywords = {Diphosphoglyceric Acids, Genetic Variation, Hemoglobins, Abnormal, Humans, Hydrogen-Ion Concentration, Oxygen, Peptide Fragments, Phytic Acid, Protein Binding}, issn = {0006-3002}, author = {Imai, K and Lehmann, H} }