PMID: 88Dec 15, 1975

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

Biochimica Et Biophysica Acta
K Imai, H Lehmann

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.

Citations

May 15, 2009·International Journal of Hematology·Noppacharn UaprasertPranee Sutcharitchan
Jan 1, 1977·Hemoglobin·L E Lie-InjoD Peterson
Jan 1, 1987·Hemoglobin·S Fucharoen, P Winichagoon
Jan 1, 1978·Hemoglobin·H F Bunn
Dec 25, 1984·Journal of Molecular Biology·W F Moo-PennA Arnone
Mar 7, 2003·Journal of Pediatric Hematology/oncology·Voravarn S TanphaichitrPanutsaya Tientadakul

Related Concepts

Diphosphoglyceric Acids
Abnormal Hemoglobins
Hydrogen-Ion Concentration
Dioxygen
Peptide Fragments
Phytate
Plasma Protein Binding Capacity
Variation (Genetics)

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