1987
DOI: 10.1016/0167-4838(87)90274-3
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Purification and some properties of peroxidases of rat bone marrow

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Cited by 36 publications
(18 citation statements)
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“…As reported previously, rat bone marrow con tains two peroxidases, namely, myeloperoxi dase and eosinophil peroxidase (9). Because KI is a good substrate for eosinophil peroxi dase and the activity of myeloperoxidase using KI as the substrate is very low, the ac tivity toward KI is thought to be due to eosinophil peroxidase, but not myeloperoxi dase (9).…”
Section: Discussionmentioning
confidence: 83%
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“…As reported previously, rat bone marrow con tains two peroxidases, namely, myeloperoxi dase and eosinophil peroxidase (9). Because KI is a good substrate for eosinophil peroxi dase and the activity of myeloperoxidase using KI as the substrate is very low, the ac tivity toward KI is thought to be due to eosinophil peroxidase, but not myeloperoxi dase (9).…”
Section: Discussionmentioning
confidence: 83%
“…As reported previously, rat bone marrow con tains two peroxidases, namely, myeloperoxi dase and eosinophil peroxidase (9). Because KI is a good substrate for eosinophil peroxi dase and the activity of myeloperoxidase using KI as the substrate is very low, the ac tivity toward KI is thought to be due to eosinophil peroxidase, but not myeloperoxi dase (9). When KI was used as the electron donor, the peroxidase activity of male WKY was higher than that of SHR and SHR-SP, suggesting that the bone marrow of male SH R and SHR-SP contain a lower activity of eosinophil peroxidase compared with WKY.…”
Section: Discussionmentioning
confidence: 95%
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