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A35Cl--NMR study of the singular anion-binding properties of dromedary hemoglobin
Linköping University, Department of Medical and Health Sciences, Division of Radiological Sciences. Linköping University, Faculty of Health Sciences. Linköping University, Center for Medical Image Science and Visualization (CMIV). Region Östergötland, Center for Surgery, Orthopaedics and Cancer Treatment, Department of Radiation Physics. Department of Biological Sciences, University of Calgary, Calgary Canada.ORCID iD: 0000-0001-8661-2232
Department of Biological Sciences, University of Calgary, Calgary Canada.
Department of Physical Chemistry 2, University of Lund, Lund Sweden.
Department of Physical Chemistry 2, University of Lund, Lund Sweden.
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1989 (English)In: Biochimica et Biophysica Acta, ISSN 0006-3002, E-ISSN 1878-2434, Vol. 999, no 1, 12-8 p.Article in journal (Refereed) Published
Abstract [en]

35Cl(-)-NMR measurements of chloride binding to carbonmonoxy- and deoxy-dromedary hemoglobin reveal the existence of two classes of chloride-binding sites, one of high and the other of low affinity. Although this situation resembles that described for human hemoglobin, it was found that the number of binding sites as well as the association equilibrium constant for chloride binding are significantly higher in the dromedary protein. This difference may be due to the greater number of basic residues exposed to solvent and to the higher flexibility of dromedary hemoglobin. The two oxygen-linked polyanion-binding sites characteristic of this hemoglobin show competition for some of the high-affinity chloride-binding sites in keeping with their location in the cleft enclosed by the beta chains and between the alpha chains termini. It is suggested that the observed anion-binding properties of dromedary hemoglobin may contribute to the control of the physiological osmotic shock after rehydration.

Place, publisher, year, edition, pages
1989. Vol. 999, no 1, 12-8 p.
Keyword [en]
Animals, Binding Sites, Camels/*blood, Carboxyhemoglobin/*metabolism, Chlorides/*metabolism, Hemoglobins/*metabolism, Hydrogen-Ion Concentration, Magnetic Resonance Spectroscopy
National Category
Physical Chemistry
Identifiers
URN: urn:nbn:se:liu:diva-114171DOI: 10.1016/0167-4838(89)90022-8OAI: oai:DiVA.org:liu-114171DiVA: diva2:790789
Note

0006-3002 (Print) Journal Article Research Support, Non-U.S. Gov't

Available from: 2015-02-25 Created: 2015-02-11 Last updated: 2017-12-04Bibliographically approved

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Lundberg, Peter

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