Respiratory burst oxidase from human neutrophils: purification and some properties.
The respiratory burst oxidase of human neutrophils was purified by "dye-affinity" chromatography over a red agarose column. Electrophoresis of the purified enzyme on NaDodSO4 gel showed a single major band at 64,000-66,000 daltons, together with some minor contaminants. On a nondenaturing gel, the e...
Uloženo v:
| Vydáno v: | Proc Natl Acad Sci U S A |
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| Hlavní autoři: | , , |
| Médium: | Artigo |
| Jazyk: | Inglês |
| Vydáno: |
National Academy of Sciences
1985
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| Témata: | |
| On-line přístup: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC397731/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/3858811/ https://ncbi.nlm.nih.govhttps://doi.org/10.1073/pnas.82.10.3144 |
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