Purification and characterization of a dipeptidase from Lactobacillus sake.
A dipeptidase was purified from cell extracts of Lactobacillus sake. This compound was a monomer having a molecular weight of 50,000 and a pI of 4.7 and exhibited broad specificity against all dipeptides except those with proline or glycine at the N terminus. The enzyme was inhibited by EDTA or 1,10...
Uloženo v:
| Vydáno v: | Appl Environ Microbiol |
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| Hlavní autoři: | , , , |
| Médium: | Artigo |
| Jazyk: | Inglês |
| Vydáno: |
American Society for Microbiology (ASM)
1995
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| Témata: | |
| On-line přístup: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC167347/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/7574624/ https://ncbi.nlm.nih.govhttps://doi.org/10.1128/aem.61.2.837-839.1995 |
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