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...

Täydet tiedot

Bibliografiset tiedot

Julkaisussa:	Appl Environ Microbiol
Päätekijät:	Shao, W, Yüksel, G U, Dudley, E G, Parkin, K L, Steele, J L
Aineistotyyppi:	Artigo
Kieli:	Inglês
Julkaistu:	American Society for Microbiology (ASM) 1997
Aiheet:	Research Article
Linkit:	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
Tagit:	Lisää tagi Ei tageja, Lisää ensimmäinen tagi!