Publications by authors named "Bidaud M"

Tuberculous aneurysms of aorta are rare. They expose to a very high risk of unpredictable rupture with serious hemodynamic consequences. We report a 82-year-old male who presented with an tuberculous aortic aneurysm in a prerupture state.

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Background And Aims Of The Study: Manual decalcification of the aortic valve was performed systematically in a prospective series of patients with asymptomatic moderate aortic stenosis (AS) undergoing coronary artery bypass grafting (CABG). This study addressed two main issues: (i) whether aortic valve decalcification is a good option to relieve moderate AS; and (ii) whether the natural progression of AS may be delayed by manual valve debridement when surgery is indicated for coronary disease.

Methods: Between October 1997 and March 2001, 14 adult patients with moderate AS underwent concomitant surgical repair of the aortic valve during CABG.

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The theory and the methods that have been described in the two preceding papers in this journal have been used to analyze the kinetic properties of chloroplast fructose bisphosphatase. The enzyme is a tetramer made up of apparently identical subunits and displays a sigmoidal kinetics with respect to its substrate, fructose bisphosphate. The free ionic species, magnesium and fructose bisphosphate bind to the enzyme and the chelate fructose-bisphosphate-magnesium does not affect the sigmoidicity of the rate curves.

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The nucleotide sequence of Pseudomonas aeruginosa phoB was determined. The sequence data suggest that the PhoB polypeptide consists of 229 amino acid residues and has a predicted molecular weight of 25,708. In the regulatory region of the gene, a very well conserved phosphate box was found.

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The complete nucleotide sequence of the colicinogenic plasmid ColA has been determined. The plasmid DNA consists of 6720 bp (molecular weight 4.48 X 10(6].

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If the conformational transition involved in enzyme memory occurs in several elementary steps, the time constant of the overall 'slow' relaxation is mostly determined by the individual values of the rate constants pertaining to the overall transconformation. The extent of kinetic co-operativity of the enzyme reaction, however, is mostly controlled by the degree of reversibility of the elementary steps of the conformational transition. There is then no simple relation between the time scale of the 'slow' transition and the extent of kinetic co-operativity of the enzyme reaction.

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