The DOI matches its Crossref record.
Interaction of hemoglobin with red blood cell membranes as shown by a fluorescent chromophore
Abstract
Hemoglobin quenching of the fluorescence intensity of 12-(9-anthroyl)stearic acid (AS) embedded in the red blood cell membrane occurs through an energy transfer mechanism and can be used to measure the binding of hemoglobin to the membrane. The binding of hemoglobin to red cell membranes was found to be reversible and electrostatic in nature. Using a theory of energy transfer based on Förster formulation, the quantitative data for the binding were derived. The number of binding sites was found to be 1.4 +/- 0.2 X 10(6) molecules per cell and the binding constant was 0.85 X 10(8) M-1.
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Citations
Cited by
Red blood cell oxidative stress impairs oxygen delivery and induces red blood cell aging
Mohanty, J. G., Nagababu, E., & Rifkind, J. M. (2014) · Frontiers in Physiology · doi:10.3389/fphys.2014.00084 · Cited by 595
The interaction of hemin and bilirubin with the human red cell membrane
Kirschner-Zilber, I., Rabizadeh, E., & Shaklai, N. (1982) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/0005-2736(82)90234-6 · Cited by 70
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Metadata
- Authors
- Shaklai, N., Yguerabide, J., & Ranney, H. M.
- Venue
- Biochemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 1977-12-13
- Volume
- 16
- Issue
- 25
- Pages
- 5585-5592
- ISSN
- 0006-2960 (ISSN-L)
- 1520-4995
- OpenAlex
- W2004938306
- Cited by
- 233
- References
- 0
- FWCI
- 3.88
- Type
- journal article
- Language
- en
- Open access
- closed
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- CoChat. (2026). Citation check: Interaction of hemoglobin with red blood cell membranes as shown by a fluorescent chromophore. https://app.cochat.ai/papers/10.1021/bi00644a031
- The paper
- Shaklai, N., Yguerabide, J., & Ranney, H. M. (1977). Interaction of hemoglobin with red blood cell membranes as shown by a fluorescent chromophore. Biochemistry. https://doi.org/10.1021/bi00644a031
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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