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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...
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| Hlavní autoři: | , , |
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| Médium: | Artigo |
| Jazyk: | Inglês |
| Vydáno: |
1971
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| Témata: | |
| On-line přístup: | https://ncbi.nlm.nih.gov/pmc/articles/PMC246907/ https://ncbi.nlm.nih.gov/pubmed/4327508 |
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