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Biomedical subjects

M Barthelemy

Publications and source records attributed to M Barthelemy.

At least 19 recordsLinked to original sources
PubMed1987

Torsade de pointes during loading with amiodarone.

Torsade de pointes represents a potential complication of chronic amiodarone therapy. Several reports have emphasized the need for a loading dose in order to achieve therapeutic blood levels rapidly. We report a case of torsade de pointes following a single oral dose of amiodarone (1400 mg or 30 mg kg-1) administered after short intravenous loading for prevention of paroxysmal atrial flutter. Torsades de pointes were preceded and associated with marked QT prolongation and bradycardia. This report suggests that careful monitoring of patients undergoing oral amiodarone loading is necessary.

Administration, Oral↗
PubMed1986

Classification of beta-lactamases from Branhamella catarrhalis in relation to penicillinases produced by other bacterial species.

Branhamella catarrhalis strains resistant to commonly used penicillins, and presently isolated, produce a beta-lactamase. Most of these enzymes are chromosomally mediated, but a plasmid-mediated beta-lactamase has been described (enzyme BRO-1). With reference to isoelectric points, 7 different enzymes have been identified: 6 chromosomally mediated and 1 plasmid-mediated. Nevertheless, they have many common properties, such as being biosynthesised constitutively but with a low level of production. They have a penicillinase-type profile, and are strongly inhibited by clavulanic acid.

Bacteria↗
PubMed1985

[Cochleo-vestibular attacks of viral origin].

The viral etiology of some cochlear or vestibular lesions is well documented. Concerning the cochlear congenital lesions, the cytomegalovirus is becoming the main etiologic factor, while the rubella vaccination has shown its efficiency in the United States. The acquired hearing or vestibular diseases were briefly reviewed as well as the pathology and their therapeutic considerations.

Cochlea↗
PubMed1978

Beta-lactamases: determination of their isoelectric points.

Important discrepancies in isoelectric points (pI) of beta-lactamases were observed depending on the experimental procedure used for their determination: isoelectric focusing (IEF) in sucrose density gradients or analytical IEF in thin-layer polyacrylamide gels (PA). The variations, negligable in the case of TEM-like beta-lactamases, appeared to be important in the case of cephalosporinases and are related to an artifact which appears in PA-IEF. This has been clearly shown with beta-lactamase preparations from the following bacterial strains: Pseudomonas aeruginosa NCTC 8203 (pI = 8.7), P. aeruginosa NCTC 10701 (pI = 9.4), and Proteus morganii NCTC 235 (pI = 8.3). The data previously obtained by PA-IEF were much lower.

Amidohydrolases↗
PubMed1978

Novel beta-lactamase from Branhamella catarrhalis.

A strain of Branhamella catarrhalis isolated from sputum was shown to be resistant to penicillin and ampicillin. This strain produced a beta-lactamase which has been judged to be a novel enzyme, on the basis of substrat profil, isoelectric point and location of genetic determinant.

Ampicillin↗
PubMed1977

[Incidence of metabolic acidosis during status asthmaticus in adults. Physiopathological consideration].

In the course of 28 cases of status asthmaticus in adults, the authors noted the frequency of metabolic acidosis, assessed as a base deficit. This disorder, already noted by other authors, remains poorly explained. It may nevertheless be conceived that its onset is favourised by the special haemodynamic consequences of this particular form of acute respiratory insufficiency.

Acidosis↗
PubMed1977

Beta-lactamases produced by a Pseudomonas aeruginosa strain highly resistant to carbenicillin.

A Pseudomonas aeruginosa strain isolated at Besançon Hospital, France, proved to be highly resistant to carbenicillin and showed a high hydrolytic activity toward this antibiotic. We clearly demonstrated that two beta-lactamases were synthetized: one of them, constitutive, has its enzymatic activity directed mainly toward penicillins, and carbenicillin appears to be its best substrate (higher V(max)); thus, this beta-lactamase is a "carbenicillinase" that differs from the well-known "TEM-like" enzymes. The isoelectric point of this carbenicillinase is 5.30 +/- 0.03. The other one is an inducible cephalosporinase, very similar to the cephalosporinases usually found in these organisms. Its isoelectric point is 8.66 +/- 0.04. These two enzymes have been separated by affinity chromatography and isoelectric focusing. The kinetic constants were measured by computerized microacidimetry.

Amidohydrolases↗
PubMed1977

[Microheterogeneity of R plasmid coded beta-lactamases in analytical isoelectric focusing (author's transl)].

Analytical isoelectric focusing of plasmid-coded beta-lactamases in polyacrylamide gels gives rise to several satellite bands in addition to one major active band (microheterogeneity). When the R plasmids are transferred by conjugation into 4 different bacterial species (Escherichia coli, Klebsiella pneumoniae, Salmonella typhi-murium, Proteus mirabilis) the position of the main band remains constant, but the number and position of the satellite bands are changed. Furthermore, the minimal inhibitory concentrations of several beta-lactamines are also changed when the plasmids are transferred between these different host strains. These facts suggest that the bacterial host might modify the physical structure and the activity of plasmid-determined beta-lactamases. They also suggest that identification of beta-lactamases and comparison of their isoelectric focusing patterns should always be carried out using the same bacterial host strain.

Amidohydrolases↗