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Human eosinophil pe...
Human eosinophil peroxidase : purification and characterization
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- Carlson, M (författare)
- Uppsala universitet,Institutionen för medicinska vetenskaper
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- Peterson, C G (författare)
- Uppsala universitet,Institutionen för medicinska vetenskaper
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- Venge, P (författare)
- Uppsala universitet,Institutionen för medicinska vetenskaper
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(creator_code:org_t)
- 1985
- 1985
- Engelska.
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Ingår i: Journal of Immunology. - 0022-1767 .- 1550-6606. ; 134:3, s. 1875-1879
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Abstract
Ämnesord
Stäng
- 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.
Nyckelord
- Amino Acids/analysis
- Antigen-Antibody Reactions
- Chromatography; Gel
- Eosinophil Peroxidase
- Eosinophilia/enzymology
- Eosinophils/*enzymology
- Humans
- Immunodiffusion
- Leukocyte Count
- Molecular Weight
- Peroxidases/analysis/*isolation & purification/metabolism
- Radioimmunoassay
- Research Support; Non-U.S. Gov't
- MEDICINE
- MEDICIN
Publikations- och innehållstyp
- ref (ämneskategori)
- art (ämneskategori)
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