Partial Purification and Properties of a Highly Specific Trehalose Phosphate Phosphatase from Mycobacterium smegmatis
A specific trehalose phosphate phosphatase was purified approximately 50-fold from Mycobacterium smegmatis. The enzyme had a pH optimum of about 7.0 and was stimulated by Mg(2+). The optimum concentration of Mg(2+) was about 1.5 × 10(−3)m. Of other divalent cations tested, only Co(2+) showed some ac...
محفوظ في:
| الحاوية / القاعدة: | J Bacteriol |
|---|---|
| المؤلفون الرئيسيون: | , , |
| التنسيق: | Artigo |
| اللغة: | Inglês |
| منشور في: |
American Society for Microbiology (ASM)
1971
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| الموضوعات: | |
| الوصول للمادة أونلاين: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC246907/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/4327508/ https://ncbi.nlm.nih.govhttps://doi.org/10.1128/jb.107.1.217-222.1971 |
| الوسوم: |
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