Wordt geladen...
Purification and properties of the 5,10-methenyltetrahydromethanopterin cyclohydrolase from Methanobacterium thermoautotrophicum.
The 5,10-methenyltetrahydromethanopterin cyclohydrolase of Methanobacterium thermoautotrophicum was purified 128-fold to homogeneity. The enzyme had a subunit Mr of 41,000 as indicated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. From high-performance size exclusion chromatography o...
Bewaard in:
| Hoofdauteurs: | , , |
|---|---|
| Formaat: | Artigo |
| Taal: | Inglês |
| Gepubliceerd in: |
1986
|
| Onderwerpen: | |
| Online toegang: | https://ncbi.nlm.nih.gov/pmc/articles/PMC213648/ https://ncbi.nlm.nih.gov/pubmed/3782039 |
| Tags: |
Voeg label toe
Geen labels, Wees de eerste die dit record labelt!
|