| Literature DB >> 3734462 |
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.Entities:
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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