Purification and characterization of the extracellular alpha-amylase from Clostridium acetobutylicum ATCC 824.
The extracellular alpha-amylase (1,4-alpha-D-glucanglucanohydrolase; EC 3.2.1.1) from Clostridium acetobutylicum ATCC 824 was purified to homogeneity by anion-exchange chromatography (mono Q) and gel filtration (Superose 12). The enzyme had an isoelectric point of 4.7 and a molecular weight of 84,00...
Αποθηκεύτηκε σε:
| Εκδόθηκε σε: | Appl Environ Microbiol |
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| Κύριοι συγγραφείς: | , , , |
| Μορφή: | Artigo |
| Γλώσσα: | Inglês |
| Έκδοση: |
American Society for Microbiology (ASM)
1991
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| Θέματα: | |
| Διαθέσιμο Online: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC182687/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/8967771/ https://ncbi.nlm.nih.govhttps://doi.org/10.1128/aem.57.1.212-218.1991 |
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