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Proceedings Paper

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
Author(s): Kazunori Kawasaki; Hellmut Merkle; Akihiro Kusumi
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Paper 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).

Paper Details

Date Published: 24 June 1988
PDF: 2 pages
Proc. SPIE 0909, Time-Resolved Laser Spectroscopy in Biochemistry, (24 June 1988); doi: 10.1117/12.945427
Show Author Affiliations
Kazunori Kawasaki, Medical College of Wisconsin (United States)
Hellmut Merkle, Medical College of Wisconsin (United States)
Akihiro Kusumi, Kyoto University (Japan)


Published in SPIE Proceedings Vol. 0909:
Time-Resolved Laser Spectroscopy in Biochemistry
Joseph R. Lakowicz, Editor(s)

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