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ISOLATION AND PURIFICATION OF MYELOPEROXIDASE FROM HUMAN POLYMORPHONEUCLEAR-CELLS (PMN) | ||
| IRAQI JOURNAL OF MEDICAL SCIENCES | ||
| Article 1, Volume 4, Issue 2, 2005, Pages 129-133 | ||
| Authors | ||
| Essam F.A. Al-Jumaily; Muntaha A.K. Al-Safar; Rhagad A.A. AlSuhail | ||
| Abstract | ||
| Background: Myeloperoxidase (MPO) oxidoreductase, EC.1.11.1.7 stored in granules of neutrophils ingest microorganisms by generating of reactive oxidants. Objective: Isolation and Purification of (MPO) from polymorphonuclear cells. Methods: The enzyme was purified from polymorphonuclear blood cells by Ion exchange chromatography by CMC and gel filtration Sephacryl S.200 column and SDS electrophoresis. Results: Polymorphonuclear cell (PMN) were isolated from human blood; cell extract was prepared by homogenizetion of cell pellets in 0.34 M sucrose. Human (PMN) Myeloperoxidase (MPO) has been purified to homogeneity by two- steps procedure, which included CM-cellulose ion exchange chromatography and Sephacyl S- 200 column at purification fold and recovery of 1.281 and 43.94% respectively. The final product was homogeneous when examined by SDS -polyacrylamide gel electrophoresis. The molecular weight of the enzyme is 80,000 daltons as determined by SDS- PAGE and 88,000 daltons by Sephacyl S-200. Conclusion: The purification of MPO with accepted yield may open new approaches for its using in the medical application as preparing of monclonal antibodies and diagnostic kits for detection of antimyeloperxidase that are required for some inflammatory diseases Keywords: Polymorphonulear cells; Myeloperoxidase | ||
| Keywords | ||
| Polymorphonulear cells; Myeloperoxidase | ||
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