Abstract
Two fluorescent probes, N-carboxymethylisatoic anhydride, which binds to membrane proteins, and 1,6-diphenyl-1,3,5-hexatriene, a lipophilic label, have been used to follow membrane microenvironmental changes. Activation of human platelets by thrombin resulted in a simultaneous increase in values of fluorescence polarization (P) of both probes during the stages of shape change and secretion, which further increased during platelet aggregation. The similar pattern of changes in P for both probes indicates the interdependence of lipids and proteins in the activated platelet membrane.
Original language | English |
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Pages (from-to) | 417-421 |
Number of pages | 5 |
Journal | Biochimica et Biophysica Acta - Biomembranes |
Volume | 598 |
Issue number | 2 |
DOIs | |
State | Published - 23 May 1980 |
Keywords
- Aggregation
- Fluorescence polarization
- Membrane protein
- Platelet
- Secretion
- Thrombin
ASJC Scopus subject areas
- Biophysics
- Biochemistry
- Cell Biology