IDENTIFICATION OF A MAJOR BASIC PROTEIN IN GUINEA PIG EOSINOPHIL GRANULES

doi:10.1084/jem.137.6.1459

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IDENTIFICATION OF A MAJOR BASIC PROTEIN IN GUINEA PIG EOSINOPHIL GRANULES

Gerald J. Gleich ¹, David A. Loegering ¹, and Jorge E. Maldonado ¹

¹ From the Department of Medicine, Sections of Allergy and Hematology, the Allergic Diseases Research Laboratory, and the Hematologic Electron Microscopy Laboratory, Mayo Foundation, Rochester, Minnesota 55901

Elucidation of the functions of the eosinophil might be accomplishedby analysis of the granule constituents. We have purified eosinophils(93% or greater) from the peritoneal cavity of the guinea pigand have investigated a variety of methods to disrupt cellsand liberate intact granules. Lysis in 0.34 M sucrose gave thebest yield of granules and these had the characteristic morphologyof eosinophil granules when examined by electron microscopy.Granules were solubilized by a variety of treatments and thesolutions analyzed by polyacrylamide electrophoresis at pH 3in 6 M urea. Comparison of the electrophoretic patterns of solubilizedeosinophil and neutrophil granules revealed a difference: amajor portion (53±3%; x ±1 SE) of the protein fromthe eosinophil granule migrated as a single component. Thismajor band protein has a molecular weight between 6,000 and12,000 daltons and a pI of 10 or greater. Analysis of eosinophilgranule constituents on Sephadex G-50 revealed two main peaks;peak 1 possessed peroxidase activity and peak 2 contained themajor band protein. These studies indicate that eosinophil granulescontain a cationic protein of low molecular weight which lacksperoxidase activity and which accounts for greater than 50%of granule protein.

Submitted on February 4, 1973

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