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Updated: Aug 2, 2026

Analysis of Cap-binding Proteins in Human Cells Exposed to Physiological Oxygen Conditions
Published on: December 28, 2016
Band-3 protein function in human erythrocytes: effect of oxygenation-deoxygenation
Antonio Galtieri1, Ester Tellone, Leonardo Romano
1Dipartimento di Chimica Organica e Biologica, Università di Messina, Messina, Italy.
Abstract:
Sulfate transport by band-3 protein in adult human erythrocytes was shown to be modulated by oxygen pressure. In particular, a higher transport activity was measured under high oxygen pressure than at low one (0.0242+/-0.0073 vs. 0.0074+/-0.0010 min(-1)). Other factors, such as magnesium ions and orthovanadate, which can indirectly affect the binding properties of the cytoplasmic domain of band 3 (cdb3), influence significantly the anion exchanger activity. No effect of oxygen pressure on sulfate transport was found in chicken erythrocytes, which may be related to their lacking the cdb3 binding site. These findings are fully consistent with a molecular mechanism where the oxygen-linked transition of hemoglobin (T-->R) could play a key role in the regulation of anion exchanger activity.
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