| Literature DB >> 88 |
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.Entities:
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Year: 1975 PMID： 88 DOI： 10.1016/0005-2795(75)90043-4
Source DB: PubMed Journal: Biochim Biophys Acta ISSN： 0006-3002