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The oxygen affinity of haemoglobin Tak, a variant with an elongated beta chain.
Metadata
JournalBiochim. Biophys. ActaNot FoundDate
1975-Dec-15
Publication Type
Journal Article
Volume
1975-Dec-15 / 412 : 288-94
Author
Imai K , Lehmann H
DoiPMIDMESH
Diphosphoglyceric Acids
Genetic Variation
Hemoglobins, Abnormal
Humans
Hydrogen-Ion Concentration
Oxygen
Peptide Fragments
Phytic Acid
Protein Binding
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.
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