Literature DB >> 3734462

A simple procedure for the purification of eosinophil peroxidase from normal human blood.

R Menegazzi, G Zabucchi, P Patriarca.   

Abstract

A simple procedure to purify human eosinophil peroxidase (EPO) is described. The method uses pure anucleated granule-rich eosinophil fragments (cytosomes) as a suitable starting material from which EPO can be quickly isolated. The enzyme obtained by this procedure has both the biochemical and the spectral properties of EPO and shows a reasonable degree of purity, as judged by its rz value. This procedure, besides its simplicity and reproducibility, offers at least two other advantages over the methods currently used for EPO purification, the possibility of isolating EPO from small amounts of normal human blood and a very high recovery of the enzyme activity.

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Year:  1986        PMID: 3734462     DOI: 10.1016/0022-1759(86)90491-6

Source DB:  PubMed          Journal:  J Immunol Methods        ISSN: 0022-1759            Impact factor:   2.303


  3 in total

1.  Myeloperoxidase exerts microbicidal activity against Mycobacterium tuberculosis.

Authors:  V Borelli; E Banfi; M G Perrotta; G Zabucchi
Journal:  Infect Immun       Date:  1999-08       Impact factor: 3.441

2.  Mutual influence between eosinophil peroxidase (EPO) and neutrophils: neutrophils reversibly inhibit EPO enzymatic activity and EPO increases neutrophil adhesiveness.

Authors:  G Zabucchi; R Menegazzi; R Cramer; E Nardon; P Patriarca
Journal:  Immunology       Date:  1990-04       Impact factor: 7.397

3.  Human eosinophil peroxidase induces surface alteration, killing, and lysis of Mycobacterium tuberculosis.

Authors:  Violetta Borelli; Francesca Vita; Sandeep Shankar; Maria Rosa Soranzo; Elena Banfi; Giuditta Scialino; Cristiana Brochetta; Giuliano Zabucchi
Journal:  Infect Immun       Date:  2003-02       Impact factor: 3.441

  3 in total

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