Biomedical subjects

C Fusté

Publications and source records attributed to C Fusté.

4 recordsLinked to original sources

PubMed1996

Outer membrane permeability of non-typable Haemophilus influenzae.

The permeability to cephaloridine was studied in five Haemophilus influenzae strains (four non-typable and one type b) using the Zimmermann and Rosselet method. The beta-lactamase activity was due to a plasmid-encoded TEM-1 enzyme. High permeability coefficients were measured in all strains examined. No great differences in permeability coefficients were found, even between strains with marked differences in OMP electrophoretic profiles.

Bacterial Typing Techniques↗

PubMed1993

Outer membrane proteins from Serratia marcescens.

The outer membrane proteins (OMPs) of several strains of Serratia marcescens have been studied by sodium dodecyl sulphate - urea - polyacrylamide gel electrophoresis. Four major OMPs, named Omp1, Omp2, Omp3, and OmpA (42, 40, 39, and 37 kDa, respectively), have been visualized. The relative proportions of Omp2 and Omp3 depend on cultural conditions (temperature of incubation, osmolarity, and nutrient availability).

Bacterial Outer Membrane Proteins↗

PubMed1992

Epidemiology and molecular basis of penicillin-resistant Neisseria meningitidis in Spain: a 5-year history (1985-1989).

Penicillin-resistant (penr) clinical isolates of Neisseria meningitidis, which do not produce beta-lactamase, were first identified in Spain in 1985; the frequency of their recovery, which has been increasing in the past few years, reached 20% in 1989. Serogrouping, determination of serotypes and subtypes, and multilocus enzyme electrophoresis of the penr strains showed an extensive diversity. Resistance is due, at least in part, to a decreased affinity of penicillin-binding protein (PBP) 2 for penicillin. Similar low-affinity forms of PBP 2 are also found in penr isolates of Neisseria lactamica, Neisseria polysaccharea, and Neisseria gonorrhoeae. Genetic transformation of an N. meningitidis type strain to low-level penicillin resistance with DNA from resistant meningococci and other Neisseria species resulted in transformants that possessed low-affinity forms of PBP 2. These altered forms of PBP 2 have been shown to arise from recombinational events that replace parts of the PBP 2 gene with the corresponding regions from the PBP 2 genes of commensal Neisseria species.

Bacterial Proteins↗

PubMed1986

Production and Rheological Properties of the Extracellular Polysaccharide Synthesized by Pseudomonas sp. Strain EPS-5028.

During batch aerobic submerged fermentation, the exopolysaccharide synthesis by Pseudomonas sp. strain EPS-5028 occurred in growth- and non-growth-linked processes. Polysaccharide formation increased when the pH was controlled at 7 during fermentation. Exopolysaccharide production depended on the phosphate content of the medium. The polymer exhibited a pseudoplastic nature, had good thermostability, and was affected neither by pH nor by high concentrations of salt.

Journal Article↗