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Slow internal dynamics of membrane proteins in mechanisms of protease‐induced aggregation of platelets
Author(s) -
Mazhul V,
Chernovets T,
Zaitseva E,
Shcharbin D
Publication year - 2003
Publication title -
cell biology international
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.932
H-Index - 77
eISSN - 1095-8355
pISSN - 1065-6995
DOI - 10.1016/s1065-6995(03)00098-2
Subject(s) - chemistry , protease , platelet , trypsin , context (archaeology) , thrombin , biophysics , tryptophan , kinetics , membrane , biochemistry , enzyme , biology , amino acid , immunology , paleontology , physics , quantum mechanics
Room temperature tryptophan phosphorescence (RTTP) of suspensions of human platelets was studied. RTTP spectra and decay kinetics of both intact platelets and those after short‐term incubation with low concentrations of thrombin or trypsin (0.3–50 μg/ml) were investigated. Protease‐induced changes in the RTTP lifetime of platelets were observed, and interpreted in terms of the slow internal dynamics of membrane protein modification. The functional role of membrane protein internal dynamics is discussed in the context of platelet aggregation and signal transduction processes.