Alteration of specific activity and stability of thermostable neutral protease by site-directed mutagenesis.
On the basis of three-dimensional information, many amino acid substitutions were introduced in the thermostable neutral protease (NprM) of Bacillus stearothermophilus MK232 by site-directed mutagenesis. When Glu at position 143 (Glu-143), which is one of the proposed active sites, was substituted f...
محفوظ في:
| الحاوية / القاعدة: | Appl Environ Microbiol |
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| المؤلفون الرئيسيون: | , , , |
| التنسيق: | Artigo |
| اللغة: | Inglês |
| منشور في: |
American Society for Microbiology (ASM)
1992
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| الموضوعات: | |
| الوصول للمادة أونلاين: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC183176/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/1482198/ https://ncbi.nlm.nih.govhttps://doi.org/10.1128/aem.58.11.3779-3783.1992 |
| الوسوم: |
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