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Purification and Partial Characterization of a Prolyl-Dipeptidyl Aminopeptidase from Lactobacillus helveticus CNRZ 32

X-prolyl-dipeptidyl aminopeptidase, which hydrolyzed Gly-Pro-p-nitroanilide (relative activity [RA] = 100%) and Arg-Pro-p-nitroanilide (RA, 130%), was purified to homogeneity from the cell extract of Lactobacillus helveticus CNRZ 32. The enzyme also hydrolyzed Ala-Pro-Gly (RA, 11%) and Ala-Ala-p-nit...

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Detalles Bibliográficos
Publicado en:Appl Environ Microbiol
Principais autores: Khalid, Noraini M., Marth, Elmer H.
Formato: Artigo
Idioma:Inglês
Publicado: American Society for Microbiology (ASM) 1990
Assuntos:
Acceso en liña:https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC183349/
https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/16348113/
https://ncbi.nlm.nih.govhttps://doi.org/10.1128/aem.56.2.381-388.1990
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