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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
 
 
 
 

Purification of horse eosinophil peroxidase.

Eosinophil peroxidase (donor: hydrogen-peroxidase oxidoreductase, EC 1.11.1.7) was isolated in a highly purified form (415/280 nm ratio, 1.05) from horse peripheral blood eosinophil. Eosinophil peroxidase was extracted from intact eosinophils (98-100% purity) or isolated eosinophil granules with 0.05 M acetate buffer (pH 4.7)/0.18 M NaCl and purified by chromatography on Sephadex G-200 and carboxymethylcellulose. Final elution was with 0.05 M acetate buffer (pH 4.7)/ 1 M NaCl. Horse eosinophil peroxidase is a strongly basic protein with bacterial properties when combined with H2O2 and iodide, bromide or, to a lesser degree, chloride.[1]

References

  1. Purification of horse eosinophil peroxidase. Jörg, A., Pasquier, J.M., Klebanoff, S.J. Biochim. Biophys. Acta (1982) [Pubmed]
 
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