Association And Anchorage Of Band 3 Protein In Compartmentalized Red Blood Cell Membranes As Observed By Rotational Diffusion Measurement Using Time-Resolved Phosphorescence Anisotropy Decay

Kazunori Kawasaki; Hellmut Merkle; Akihiro Kusumi

doi:10.1117/12.945427

24 June 1988 Association And Anchorage Of Band 3 Protein In Compartmentalized Red Blood Cell Membranes As Observed By Rotational Diffusion Measurement Using Time-Resolved Phosphorescence Anisotropy Decay

Kazunori Kawasaki, Hellmut Merkle, Akihiro Kusumi

Author Affiliations +

Proceedings Volume 0909, Time-Resolved Laser Spectroscopy in Biochemistry; (1988) https://doi.org/10.1117/12.945427
Event: 1988 Los Angeles Symposium: O-E/LASE '88, 1988, Los Angeles, CA, United States

Abstract

Rotational mobility of band 3 (an anion channel protein) in human erythrocyte membranes and ghost membranes was studied to analyze band 3 self-association in the membrane and anchorage of band 3 by the cytoskeletal/peripheral protein network associated with the inner surface of the membrane. Rotational diffusion of band 3 was observed by time-resolved phosphorescence anisotropy decay of erythrosin and eosin covalently attached to band 3 (1 probe/band 3). The phosphorescence lifetimes of eosin and erythrosin attached to band 3 are approximately 2.4 and 0.4 msec, respectively. The use of both probes enabled us to observe rotational correlation times of band 3 between 10 psec and 7 msec (see Figure 1).

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Kazunori Kawasaki, Hellmut Merkle, and Akihiro Kusumi "Association And Anchorage Of Band 3 Protein In Compartmentalized Red Blood Cell Membranes As Observed By Rotational Diffusion Measurement Using Time-Resolved Phosphorescence Anisotropy Decay", Proc. SPIE 0909, Time-Resolved Laser Spectroscopy in Biochemistry, (24 June 1988); https://doi.org/10.1117/12.945427

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