| Literature DB >> 6424651 |
R Baumann, E Goldbach, E A Haller, P G Wright.
Abstract
The isolated minor haemoglobin fractions (haemoglobin D) of ostrich, chicken and duck haemoglobin, which constitute about 30% of total intracellular haemoglobin, form crystalline aggregates upon deoxygenation at physiological temperature, ionic strength and pH and at haemoglobin concentrations even well below those present in the red cell. The aggregation is reversed by oxygenation, and can be inhibited by addition of organic phosphates or the corresponding major haemoglobin fraction in a stoichiometric ratio of 1:1. Embryonic haemoglobin from chicken has similar characteristics with respect to its solubility. The results indicate close functional homology of alpha D and embryonic pi-chains as well as a novel role for organic phosphates in the regulation of haemoglobin function.Entities:
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Year: 1984 PMID： 6424651 PMCID： PMC1153280 DOI： 10.1042/bj2170767
Source DB: PubMed Journal: Biochem J ISSN： 0264-6021 Impact factor: 3.857