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PubMed · 3918110

Human eosinophil peroxidase: purification and characterization.

M G Carlson·C G Peterson·P Venge
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Abstract

Human eosinophil peroxidase (EPO) was isolated from granules from granulocytes of a patient with hypereosinophilia. The granules were extracted by means of 0.2 M NaAc, pH 4.0. The purification steps included gel filtration chromatography on Sephadex G-75 superfine and ion-exchange chromatography on CM-Sephadex G-50. The purified protein showed one band on agarose-electrophoresis, a high peroxidase activity, and a 415-nm/280 nm ratio of 1.15. After reduction, EPO showed two bands on SDS-PAGE of m.w. 52,000 and 15,000, respectively. On gel filtration, the unreduced protein had a m.w. of approximately 77,000. Amino acid analyses showed a high content of arginine and aspartic acid. Monospecific antibodies to EPO were prepared in rabbits, and a specific radioimmunoassay was developed. There was an almost linear correlation between the content of EPO measured by the radioimmunoassay and the number of eosinophils in a mixed cell extract from reference material, indicating the eosinophil origin of EPO. The content of EPO was estimated to be 15.0 micrograms/10(6) eosinophils.

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Amino AcidsAntigen-Antibody ReactionsChromatography, GelEosinophil PeroxidaseEosinophiliaEosinophilsHumansImmunodiffusionLeukocyte CountMolecular WeightPeroxidasesRadioimmunoassayJournal ArticleResearch Support, Non-U.S. Gov't

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M G Carlson, C G Peterson, P Venge. 1985. Human eosinophil peroxidase: purification and characterization.. https://pubmed.ncbi.nlm.nih.gov/3918110/

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