Spectrophotometric measurement of hemoglobin oxygen saturation in the opossum Didelphis virginiana

Spectrophotometric measurement of hemoglobin oxygen saturation in the opossum Didelphis virginiana

1. 1. A spectrophotometric method can be used to measure oxyhemoglobin dissociation in opossums at optical densities of 500 and 592 nm. 2. 2. Opossum hemoglobin spectrogram reveals a double-humped curve for oxygenated hemoglobin and a single-humped curve for reduced hemoglobin. 3. 3. The P 50 calcul...

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Veröffentlicht in:Comparative biochemistry and physiology. A, Comparative physiology Comparative physiology, 1975-02, Vol.50 (2), p.273-276
Hauptverfasser: Petty, Clayton, Bethlenfalvay, Nicholas C, Bageant, Thomas
Format: Artikel
Sprache:eng
Schlagworte:
2,3-diphosphoglycerate (2,3-DPG)
Animals
Binding Sites
Didelphis virginiana
Erythrocytes - analysis
Hemoglobins
opossum
Opossums - blood
Oxygen - blood
Oxyhemoglobin dissociation
Oxyhemoglobins
P50
Protein Binding
Protein Conformation
Spectrophotometry
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Zusammenfassung:1. 1. A spectrophotometric method can be used to measure oxyhemoglobin dissociation in opossums at optical densities of 500 and 592 nm. 2. 2. Opossum hemoglobin spectrogram reveals a double-humped curve for oxygenated hemoglobin and a single-humped curve for reduced hemoglobin. 3. 3. The P 50 calculated by the above method at pH 7·4, 35°C and 40 mm Hg P a CO 2 is 35·0 mm Hg of oxygen.
ISSN:0300-9629
DOI:10.1016/0300-9629(75)90011-0