Zobrazeno 1 - 10
of 38
pro vyhledávání: '"Tripeptide aminopeptidase"'
Autor:
Rodriguez-lllera, Marta1 marta.rodriguezillera@wur.nl, Ramires Ferreira Da Silua, Andre1, Boom, Remko M.1, Janssen, Anja E. M.1 anja.janssen@wur.nl
Publikováno v:
Food & Bioproducts Processing: Transactions of the Institution of Chemical Engineers Part C. Apr2015, Vol. 94, p255-262. 8p.
Publikováno v:
CHEST. Feb2013, Vol. 143 Issue 2, p371-378. 8p.
Akademický článek
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Autor:
Solé-Domènech, Santiago, Maxfield, Frederick R., Rojas, Ana V., Maisuradze, Gia G., Scheraga, Harold A., Lobel, Peter
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America; 2/13/2018, Vol. 115 Issue 7, p1493-1498, 6p
Selectivity mechanism of a bacterial homolog of the human drug-peptide transporters PepT1 and PepT2.
Autor:
Guettou, Fatma1, Quistgaard, Esben M1, Raba, Michael1, Moberg, Per1, Löw, Christian1, Nordlund, Pär2
Publikováno v:
Nature Structural & Molecular Biology. Aug2014, Vol. 21 Issue 8, p728-731. 4p.
Publikováno v:
Plant & Cell Physiology. Jun1997, Vol. 38 Issue 6, p759-768. 10p.
Publikováno v:
Bioscience, Biotechnology, and Biochemistry. 68:1149-1152
Four mutations observed between tripeptidases from Lactococcus lactis subsp. lactis and subsp. cremoris were introduced one by one to the corresponding points in wild-type tripeptidase from L. lactis subsp. lactis. The k(cat) values of four resultant
Autor:
Kirsi Savijoki, Airi Palva
Publikováno v:
Applied and Environmental Microbiology. 66:794-800
A tripeptidase (PepT) from a thermophilic dairy starter strain of Lactobacillus helveticus was purified by four chromatographic steps. PepT appeared to be a trimeric metallopeptidase with a molecular mass of 150 kDa. PepT exhibited maximum activity a
Publikováno v:
Scopus-Elsevier
A tripeptidase was purified to homogeneity from the cell extract of Lactobacillus sake by ammonium sulfate precipitation, hydrophobic interaction chromatography, gel filtration chromatography, and two steps of anion exchange chromatography. After SDS
Publikováno v:
Applied and Environmental Microbiology. 63:4872-4876
A tripeptidase was purified from the cytoplasm of Pediococcus pentosaceus K9.2 by anion-exchange chromatography, gel filtration chromatography, and high-performance liquid chromatography. The molecular mass of the enzyme was estimated by gel filtrati