Oxygen-dissociation properties and regulation of oxygen affinity of polymerized bovine hemoglobin
โ Scribed by E. P. Vyazova; M. A. Azhigirova; L. V. Fetisova; A. A. Khachatur'yan; G. Ya. Rozenberg
- Publisher
- Springer US
- Year
- 1983
- Tongue
- English
- Weight
- 213 KB
- Volume
- 95
- Category
- Article
- ISSN
- 0007-4888
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Dielectric properties of human and horse hemoglobin were studied at frequencies ranging from 20 kc./sec. to 7 illc./sec. The relative errors in the measurements were usually less thaii The experimental setup allowed ns variation and measurement of the degree of oxygenation of the protein and to det
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