Zobrazeno 1 - 10
of 14
pro vyhledávání: '"Iris Thamm"'
Use of an ALFexpress™ DNA Sequencer to Analyze Protein-Nucleic Acid Interactions by Band Shift Assay
Publikováno v:
BioTechniques, Vol 30, Iss 5, Pp 1044-1051 (2001)
Gel retardation analysis, or band shift assay, is technically the simplest method to investigate protein-nucleic acid interactions. In this report, we describe a nonradioactive band shift assay using a fluorescent DNA target and an ALFexpress™ auto
Externí odkaz:
https://doaj.org/article/477e43b23c144fbbb2b85402a7007513
Autor:
Paola Sandra Mercuri, Kris De Vriendt, Bart Devreese, Otto Dideberg, Iris Thamm, Jean-Marie Frère, Jozef Van Beeumen, I. Garcia-Saez, Moreno Galleni, Gian Maria Rossolini
Publikováno v:
Journal of Biological Chemistry. 279:33630-33638
The subclass B3 FEZ-1 beta-lactamase produced by Fluoribacter (Legionella) gormanii is a Zn(II)-containing enzyme that hydrolyzes the beta-lactam bond in penicillins, cephalosporins, and carbapenems. FEZ-1 has been extensively studied using kinetic,
Autor:
Patrice Filée, Jean-Marie Frère, Tony Aerts, Raphaël Herman, Christelle Vreuls, Peter Paul De Deyn, Iris Thamm, Bernard Joris
Publikováno v:
The journal of biological chemistry
In the absence of penicillin, the beta-lactamase encoding gene blaP of Bacillus licheniformis 749/I is negatively regulated by the transcriptional repressor BlaI. Three palindromic operator regions are recognized by BlaI: two in the blaP promoter (OP
Autor:
Willy Zorzi, Ana Maria Amoroso, Iris Thamm, Frédéric Sapunaric, Jacques Coyette, Colette Duez
Publikováno v:
Microbiology. 147:2561-2569
A penicillin-resistant mutant, JH2-2r (MIC 75 μg ml−1), was isolated from Enterococcus faecalis JH2-2 (MIC 5 μg ml−1) by successive passages on plates containing increasing concentrations of benzylpenicillin. A comparison of the penicillin-bind
Autor:
L. Fanuel, J. Van Beeumen, Bernard Joris, Vesna Kostanjevecki, Jean-Marie Frère, Colette Goffin, Iris Thamm, J. Brannigan, Bart Samyn
Publikováno v:
Cellular and Molecular Life Sciences CMLS. 55:812-818
Two new enzymes which hydrolyse D-alanyl-p-nitroanilide have been detected in Ochrobactrum anthropi LMG7991 extracts. The first enzyme, DmpB, was purified to homogeneity and found to be homologous to the Dap protein produced by O. anthropi SCRC C1-38
Autor:
Iris Thamm, Nicole Marty, Bernard Joris, Colette Duez, Marie-Jeanne Vacheron, Micheline Guinand, Jean-Marie Ghuysen, Martine Malissard, Georges Michel
Publikováno v:
FEMS Microbiology Letters. 110:101-106
The recombinant plasmid pAL-A3 bears a (poly ManA) alginate lyase-encoding gene that originates from the marine bacterium ATCC 433367 (Brown et al., Appl. Environ. Microbiol. (1991) 57, 1870-1872). The alginate lyase produced by Escherichia coli TC4
Autor:
Sophie Lepage, Marc Jamin, Jean-Marie Frère, Moreno Galleni, Iris Thamm, Bernard Lakaye, Bernard Joris
Publikováno v:
Biochemical Journal. 291:19-21
A new method for the identification and quantification of penicillin-binding proteins is described which uses fluorescein-coupled penicillins. It allows the rapid detection of 0.2 pmol with the naked eye and 2 fmol with the help of an A.L.F. automati
Autor:
Colette, Duez, Willy, Zorzi, Frédéric, Sapunaric, Ana, Amoroso, Iris, Thamm, Jacques, Coyette
Publikováno v:
Microbiology (Reading, England). 147(Pt 9)
A penicillin-resistant mutant, JH2-2r (MIC 75 microg ml(-1)), was isolated from Enterococcus faecalis JH2-2 (MIC 5 microg ml(-1)) by successive passages on plates containing increasing concentrations of benzylpenicillin. A comparison of the penicilli
Publikováno v:
BioTechniques. 30(5)
Gel retardation analysis, or band shift assay, is technically the simplest method to investigate protein-nucleic acid interactions. In this report, we describe a nonradioactive band shift assay using a fluorescent DNA target and an ALFexpress™ auto
Publikováno v:
DNA sequence : the journal of DNA sequencing and mapping. 9(3)
A chromosomal 10355-bp segment of Enterococcus hirae S185 contains nine orfs which occur in the same order as the MraW-, FtsL-, PBP3-, MraY-, MurD-, MurG-, FtsQ-, FtsA- and FtsZ-encoding genes of the division and cell wall clusters of Escherichia col