Purification and Mn2+ activation of Rhodospirillum rubrum nitrogenase activating enzyme.
The Fe protein activating enzyme for Rhodospirillum rubrum nitrogenase was purified to approximately 90% homogeneity, using DE52-cellulose chromatography and sucrose density gradient centrifugation. Activating enzyme consists of a single polypeptide of molecular weight approximately 24,000. ATP was...
保存先:
| 出版年: | J Bacteriol |
|---|---|
| 主要な著者: | , |
| フォーマット: | Artigo |
| 言語: | Inglês |
| 出版事項: |
American Society for Microbiology (ASM)
1982
|
| 主題: | |
| オンライン・アクセス: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC221521/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/6813313/ https://ncbi.nlm.nih.govhttps://doi.org/10.1128/jb.152.2.714-721.1982 |
| タグ: |
タグなし, このレコードへの初めてのタグを付けませんか!
|
