作者: A. S. Fauci , G. J. Gleich , Steven J. Ackerman , D. A. Loegering , J. B. Harley
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摘要: The human eosinophil granule contains a number of cationic proteins that have been identified and purified to homogeneity, including the major basic protein (MBP), (ECP), eosinophil-derived neurotoxin (EDN). Because confusion in literature regarding distinctiveness MBP ECP, we investigated immunochemical physicochemical properties these by electrophoresis on sodium dodecyl sulfate-polyacrylamide gels (SDS-PAGE), specific double antibody radioimmunoassays (RIA) for fractionation acid-solubilized granules Sephadex G-50 columns. Analysis mixture three SDS-PAGE showed they migrated as distinct bands with differing m.w. Comparison RIA ECP did not demonstrate any appreciable cross-reactivities among proteins. column fractions were analyzed analysis individual fractions. MBP, EDN eluted at different volumes from columns determined SDS-PAGE. Soluble extracts patients hypereosinophilic syndrome contained between six 64 times more than weight basis. These observations are distinctive eosinophilia contain considerably greater quantities ECP.