Biochemical and molecular characterization of PepR, a dipeptidase, from Lactobacillus helveticus CNRZ32.
A dipeptidase with prolinase activity from Lactobacillus helveticus CNRZ32, which was designated PepR, was purified to gel electrophoretic homogeneity and characterized. The NH2-terminal amino acid sequence of the purified protein had 96% identity to the deduced NH2-terminal amino acid sequence of t...
Gorde:
| Argitaratua izan da: | Appl Environ Microbiol |
|---|---|
| Egile Nagusiak: | , , , , |
| Formatua: | Artigo |
| Hizkuntza: | Inglês |
| Argitaratua: |
American Society for Microbiology (ASM)
1997
|
| Gaiak: | |
| Sarrera elektronikoa: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC168651/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/9292995/ https://ncbi.nlm.nih.govhttps://doi.org/10.1128/aem.63.9.3438-3443.1997 |
| Etiketak: |
Etiketarik gabe, Izan zaitez lehena erregistro honi etiketa jartzen!
|
