## T W O FIGURES That no two hemoglobins are quite the same was pointed out some years ago by Barcroft ('28). New evidence from many sources has confirmed his observations. Furthermore The authors wish to make acknowledgment of facilities made available f o r these studies by the U. S. Bureau of
The quaternary structure of tetrameric hemoglobin regulates the oxygen affinity of polymerized hemoglobin
โ Scribed by Andre F. Palmer; Guoyong Sun; David R. Harris
- Publisher
- American Institute of Chemical Engineers
- Year
- 2009
- Tongue
- English
- Weight
- 549 KB
- Volume
- 25
- Category
- Article
- ISSN
- 8756-7938
- DOI
- 10.1002/btpr.265
No coin nor oath required. For personal study only.
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The decrease in oxygen aflinity with increasing hemoglobin concentration, which occurs in solutions of pure hemoglobin S, can be used to determine the minimum concentration at which polymerization of the deoxy form takes place. On this basis a very sensitive method for measuring the minimum gelling
## Abstract When oxygen binds to one of the subunits of hemoglobin, the oxygen affinity of the other subunits is enhanced. This cooperative interaction of the subunits is initiated by the movement of the heme plane toward the proximal side when oxygen binds to the heme. This motion is transmitted t