Identification of elastase in human eosinophils: Immunolocalization, isolation, and partial characterization

Giuseppe Lungarella, Renzo Menegazzi, Concetta Gardi, Paola Spessotto, M. Margherita de Santi, Paolo Bertoncin, Pierluigi Patriarca, Paola Calzoni, Giuliano Zabucchi

Research output: Contribution to journalArticlepeer-review


Although an elastolytic activity in eosinophil-rich cell fractions from mice has been reported, this enzyme has not been purified and characterized as yet in any mammalian species. Eosinophilic elastase was isolated from human eosinophil fragments (cytosomes) obtained from normal and eosinophilic subjects. The enzyme was purified to apparent electrophoretic homogeneity by fast protein liquid chromatography. The enzyme shows the same physical properties of the major elastase isoenzyme of human neutrophils. In addition, like monocyte elastase, it reacts with a monoclonal antibody against human neutrophil elastase. The biochemical similarities observed between the above-mentioned enzymes and the immunolocalization findings strongly support the idea that human eosinophils and neutrophils contain the same enzyme activity. Eosinophils show immunoreactive material in both types of dense cytoplasmic granules. This observation supports the current hypothesis that the different types of eosinophilic granules represent successive morphological stages of maturation.

Original languageEnglish
Pages (from-to)128-135
Number of pages8
JournalArchives of Biochemistry and Biophysics
Issue number1
Publication statusPublished - 1992

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology


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