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Bovine hemoglobin as a basis for artificial oxygen carriers
E Bucci1, C Fronticelli, C Orth
1Dept. of Biological Chemistry, University of Maryland Medical School, Baltimore 21201.
Biomaterials, Artificial Cells, and Artificial Organs
|January 1, 1988
Summary
Bovine hemoglobin has lower oxygen affinity than human hemoglobin, especially at high salt concentrations. Bovine red blood cells, lacking 2,3-DPG, offer extended storage potential without altering oxygen affinity.
Area of Science:
- Biochemistry
- Physiology
Background:
- Hemoglobin's oxygen affinity is crucial for oxygen transport.
- Differences in hemoglobin function between species impact physiological roles and potential applications.
Purpose of the Study:
- To investigate the oxygen affinity of bovine hemoglobin compared to human hemoglobin under varying ionic conditions.
- To explore the role of chloride ions and 2,3-diphosphoglycerate (2,3-DPG) in modulating hemoglobin oxygen binding.
- To assess the stability and potential for storage of bovine red blood cells.
Main Methods:
- Comparative analysis of oxygen affinity under different pH and ionic strengths.
- Investigation of 2,3-DPG sensitivity in the presence and absence of chloride ions.
- Chemical modification of deoxy-bovine hemoglobin with 2,3-dibromo-salycyl-fumarate.
- Purification and characterization of modified hemoglobin using anion exchange and reverse phase chromatography.
- Assessment of modified hemoglobin stability and in vivo retention in rats.
Main Results:
- Bovine hemoglobin exhibits lower oxygen affinity than human hemoglobin at physiological pH and chloride concentrations, with this difference amplified at high ionic strength.
- Bovine hemoglobin's oxygen affinity is insensitive to 2,3-DPG in the presence of chloride ions, unlike human hemoglobin.
- Chemical modification of deoxy-bovine hemoglobin with 2,3-dibromo-salycyl-fumarate decreased its oxygen affinity.
- Modified tetrameric bovine hemoglobins showed resistance to dissociation at acidic pH due to intramolecular crosslinks.
- Bovine red blood cells, lacking 2,3-DPG, can be stored for extended periods in saline without significant changes in oxygen affinity.
Conclusions:
- Chloride ions play a key role in the differential oxygen affinity and 2,3-DPG response between bovine and human hemoglobin.
- The unique properties of bovine hemoglobin and red blood cells suggest potential advantages for blood storage and transfusion.
- Modulation of bovine red cell oxygen affinity is achievable through alterations in chloride ion concentration and pH.