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Cloning of the murine eosinophil peroxidase gene (mEPO): characterization of a conserved subgroup of mammalian hematopoietic peroxidases
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Cloning of the murine eosinophil peroxidase gene (mEPO): characterization of a conserved subgroup of mammalian hematopoietic peroxidases

Margaret A Horton, Kirsten A Larson, James J Lee and Nancy A Lee
Journal of leukocyte biology, v 60(2), pp 285-294
Aug 1996
PMID: 8773591

Abstract

evolution mouse eosinophils gene organization granule proteins
The mouse eosinophil peroxidase (mEPO) gene was cloned by screening a random‐primed bone marrow cDNA library at reduced criteria using a hEPO cDNA. An mEPO cDNA was subsequently used to isolate the mEPO gene from a λ‐genomic library. The mEPO gene displays a high degree of conservation with its human homologue: the transcription units are approximately the same size, conserve the relative size and position of the 12 exons associated with each gene, and at a nucleotide level the mouse and human EPO genes are 86% identical in the protein coding regions and 66% identical in the 3'‐untranslated trailer regions. This strong conservation extends to the encoded proteins which show ~90% amino acid identity. Expression of the mEPO gene is restricted to tissues containing eosinophil progenitor cells (e.g., bone marrow and spleen), a pattern similar to the expression of another murine eosinophil granule protein, major basic protein. J. Leukoc. Biol. 60: 285–294; 1996.

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Web of Science research areas
Cell Biology
Hematology
Immunology
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