Zobrazeno 1 - 10
of 17
pro vyhledávání: '"R N, Farías"'
Autor:
A, Blond, J, Péduzzi, C, Goulard, M J, Chiuchiolo, M, Barthélémy, Y, Prigent, R A, Salomón, R N, Farías, F, Moreno, S, Rebuffat
Publikováno v:
European journal of biochemistry. 259(3)
Microcin J25 (MccJ25) is the single representative of the immunity group J of the microcin group of peptide antibiotics produced by Enterobacteriaceae. It induces bacterial filamentation in susceptible cells in a non-SOS-dependent pathway [R. A. Salo
Autor:
R N Farías, R A Salomón
A chromosomal Tn5 insertion resulting in complete resistance to the peptide antibiotic microcin 25 was mapped to the min 4 region of the Escherichia coli genetic map. Additional experiments showed that the insertion disrupted the fhuA gene, which enc
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9dc8c6c31ad29b5dab84f8267e202299
https://europepmc.org/articles/PMC206939/
https://europepmc.org/articles/PMC206939/
Autor:
A N, Fanjul, R N, Farías
Publikováno v:
The Journal of biological chemistry. 268(1)
Similar cold-sensitive properties, values of dissociation constants (Kd = 1 x 10(-10) M), and regulatory effectors were found for the cold-sensitive cytosolic 3,5,3'-triiodo-L-thyronine (L-T3)-binding protein (CTBP) and pyruvate kinase from human ery
Autor:
R A Salomón, R N Farías
Publikováno v:
Journal of bacteriology. 174(22)
Microcin 25, a peptide antibiotic excreted by an Escherichia coli strain isolated from human feces, was purified to homogeneity and characterized. Composition analysis and data from gel filtration indicated that microcin 25 may contain 20 amino acid
Autor:
R N Farías, J P Fay
Publikováno v:
Applied and Environmental Microbiology. 31:153-157
Preincubation at 0 C considerably increased the bactericidal action of 0.4% nonanoic and decanoic acids on Escherichia coli K-12 154. This lethal effect seemed to be dependent on the media used to grow the bacteria. Stationary-phase cells were more s
Autor:
D de Menidoza, R N Farías
Publikováno v:
Journal of Biological Chemistry. 253:6249-6254
The influence of cold exposure at 4 degrees C for different periods of time (from 12 h to 42 days) on the allosteric inhibition by F- of the rat erythrocyte membrane-bound acetylcholinesterase from rat fed a corn oil diet was studied. The cold exposu
Publikováno v:
The Journal of biological chemistry. 258(11)
Two orders of saturable binding sites for L-triiodothyronine were found on washed rat erythrocyte membranes. The high affinity, low capacity site showed values of Kd 0.19 X 10(-10) M. This value was in the range of concentration of free L-triiodothyr
Publikováno v:
The Journal of biological chemistry. 261(33)
We have studied, by fluorescence methods, the association of insulin to liposomes, the modification of lipid fluidity, and the fusion of vesicles induced by insulin. All parameters showed a similar dependence on pH and ionic strength of the medium an
Publikováno v:
The Journal of biological chemistry. 256(14)
The action of L-triiodothyronine, L-thyroxine, and their analogues on the (Ca2+ + Mg2+)-ATPase of erythrocytes from rats fed with two different fat-supplemented diets has been studied. It was found that only L-triiodothyronine and L-thyroxine have ef
Publikováno v:
Biochimica et biophysica acta. 422(1)
Electrophoretic patterns of acetylcholinesterase (acetylcholine hydrolase, EC 3.1.1.7) from rat erythrocyte were studied. The enzyme was solubilized by the following treatments: a) Triton X-100, b) sodium deoxycholate, or c) ultrasonic irradiation. W