ArticleThe Biochemical journal1985
Further characterization of human eosinophil peroxidase.
Article in The Biochemical journal, 1985. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
5 citing papers in PubMed.
- Structural stability and heme binding potential of the truncated human dual oxidase 2 (DUOX2) peroxidase domain.Archives of biochemistry and biophysics · 2011Article
- rhEPO (recombinant human eosinophil peroxidase): expression in Pichia pastoris and biochemical characterization.The Biochemical journal · 2006Article
- Membrane peroxidases.Molecular and cellular biochemistry · 1988Review
- Cytophilic and cytotoxic properties of human eosinophil peroxidase plus major basic protein.The American journal of pathology · 1988Article
- Uptake of human eosinophil peroxidase by human neutrophils.The American journal of pathology · 1986Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The large and the small subunits (Mr 50 000 and 10 500 respectively) of human eosinophil peroxidase were isolated by gel filtration under reducing conditions. The subunits were very strongly associated but not apparently cross-linked by disulphide bridges. During storage, the large subunit tended to form aggregates, which required reduction to dissociate them. Amino acid analysis of the performic acid-treated large subunit showed the presence of 19 cysteic acid residues. The small subunit of eosinophil peroxidase had the same Mr value as the small subunit of myeloperoxidase. However, although these subunits have very similar amino acid compositions, they showed different patterns of peptide fragmentation after CNBr treatment. The carbohydrate of eosinophil peroxidase seemed associated exclusively with the large subunit and comprised mannose (4.5%, w/w) and N-acetylglucosamine (0.8%, w/w). The far-u.v.c.d. spectrum of the enzyme indicated the presence of relatively little ordered secondary structure.
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