Zobrazeno 1 - 10
of 11
pro vyhledávání: '"Paris S. T. Tan"'
Publikováno v:
Microbiology. 142:799-808
An aminopeptidase with a very broad substrate specificity was purified to homogeneity from Lactobacillus helveticus SBT 2171 by FPLC. The enzyme was purified 144-fold from a cell-free extract with a yield of 16%. The purified enzyme appeared as a sin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3d761aa66090e15ab49d7cdeffcc3ade
https://doi.org/10.1099/00221287-142-4-799
https://doi.org/10.1099/00221287-142-4-799
Publikováno v:
Journal of Dairy Research. 62:601-610
SUMMARYA total of 169Lactobacillusstrains from 12 species (Lb. acidophilus, Lb. brevis, Lb. buchneri, Lb. casei, Lb. delbrueckiisubsp.bulgaricus, Lb. delbrueckiisubsp.delbrueckii, Lb. delbrueckiisubsp.lactis, Lb. fermentum, Lb. helveticus, Lb. paraca
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::170b343e6ce039c33dfe3e9e9b1105a4
https://doi.org/10.1017/s0022029900031332
https://doi.org/10.1017/s0022029900031332
Autor:
Alfred J. Haandrikman, Odilia Velterop, Wilhelmus Konings, Kees L. Leenhouts, Gerhardus Venema, Paris S. T. Tan, Jan Kok, Igor Mierau
Publikováno v:
Journal of Bacteriology, 176(10), 2854-2861. AMER SOC MICROBIOLOGY
The gene encoding a tripeptidase (pepT) of Lactococcus lactis subsp. cremoris (formerly subsp. lactis) MG1363 was cloned from a genomic library in pUC19 and subsequently sequenced. The tripeptidase of L. lactis was shown to be homologous to PepT of S
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e6f9e93507714741dc285a4c8f2ceba9
https://doi.org/10.1128/jb.176.10.2854-2861.1994
https://doi.org/10.1128/jb.176.10.2854-2861.1994
Autor:
Paris S. T. Tan, Wn Konings
Publikováno v:
Applied and Environmental Microbiology. 56:526-532
An aminopeptidase was purified to homogeneity from a crude cell extract of Lactococcus lactis subsp. cremoris Wg2 by a procedure that included diethyl-aminoethane-Sephacel chromatography, phenyl-Sepharose chromatography, gel filtration, and high-perf
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a4d6d78ca73ebf25d288a9d7162cd864
https://doi.org/10.1128/aem.56.2.526-532.1990
https://doi.org/10.1128/aem.56.2.526-532.1990
Publikováno v:
The Journal of dairy research. 62(4)
SUMMARYCell extracts of various lactobacilli and twoLactococcusstrains were investigated for their immunoresponse with monoclonal and polyclonal antibodies raised against various proteolytic enzymes fromLc. lactis. Except forLactobacillus caseiSBT 22
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4f7c80e37b176f0968cdeb16a97baef3
https://pubmed.ncbi.nlm.nih.gov/8568031
https://pubmed.ncbi.nlm.nih.gov/8568031
Autor:
F. L. M. Van De Veerdonk, Wn Konings, Peter Frederik Zuurendonk, Paris S. T. Tan, A. P. Bruins, T. A. J. M. Van Kessel
Publikováno v:
Applied and environmental microbiology. 59(5)
The mode of action of purified aminopeptidase N from Lactococcus lactis subsp. cremoris Wg2 on a complex peptide mixture of a tryptic digest from bovine beta-casein was analyzed. The oligopeptides produced in the tryptic digest before and after amino
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a3464712610e56cefbd94532fac27e59
https://pubmed.ncbi.nlm.nih.gov/8100130
https://pubmed.ncbi.nlm.nih.gov/8100130
Autor:
Willem M. de Vos, Roland J. Siezen, Paris S. T. Tan, Ingrid van Alen-Boerrigter, Wilhelmus Konings, Bert Poolman
Publikováno v:
FEBS Letters, 306(1), 9-16. Wiley
The nucleotide sequence of the pepN gene from Lactococcus lactis encoding a zinc-metallo aminopeptidase has been determined. The open reading frame of 2,538 base pairs encodes a protein with a calculated M(r) of 95,368, which agrees with the apparent
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c15b93c66e1a6f2fff1dcd3b462c8819
https://doi.org/10.1016/0014-5793(92)80827-4
https://doi.org/10.1016/0014-5793(92)80827-4
Autor:
Micheline Rousseau, Paris S. T. Tan, Clair-Yves Boquien, Klaas M. Pos, Jean-Claude Gripon, Wil N. Konings, Marie-Pierre Chapot-Chartier
Publikováno v:
Applied and Environmental Microbiology
Applied and Environmental Microbiology, American Society for Microbiology, 1992, 58 (1), pp.285-290
Applied and environmental microbiology, 58(1), 285-290. AMER SOC MICROBIOLOGY
HAL
Applied and Environmental Microbiology, American Society for Microbiology, 1992, 58 (1), pp.285-290
Applied and environmental microbiology, 58(1), 285-290. AMER SOC MICROBIOLOGY
HAL
The localization of two aminopeptidases, an X-prolyl-dipeptidyl aminopeptidase, an endopeptidase, and a tripeptidase in Lactococcus lactis was studied. Polyclonal antibodies raised against each purified peptidase are specific and do not cross-react w
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d431c79fb8b17b6ea6720ee8d4ebb444
https://europepmc.org/articles/PMC195205/
https://europepmc.org/articles/PMC195205/
An endopeptidase has been purified to homogeneity from a crude cell extract of Lactococcus lactis subsp. cremoris Wg2 by a procedure that includes diethyl-aminoethane-Sephacel chromatography, phenyl-Sepharose chromatography, hydroxylapatite chromatog
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::313f9505a8b40980c2f98b3278987785
https://europepmc.org/articles/PMC184018/
https://europepmc.org/articles/PMC184018/
Publikováno v:
Applied and environmental microbiology. 56(6)
A tripeptidase from a cell extract of Lactococcus lactis subsp. cremoris Wg2 has been purified to homogeneity by DEAE-Sephacel and phenyl-Sepharose chromatography followed by gel filtration over a Sephadex G-100 SF column and a high-performance liqui
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::72ce1877fe6d948378a1f822a54601ed
https://pubmed.ncbi.nlm.nih.gov/16348224
https://pubmed.ncbi.nlm.nih.gov/16348224