Publications by authors named "A Karoumi"

is a waterborne pathogen that causes a severe form of pneumonia called Legionnaires' diseases, which is normally acquired by inhalation of aerosols containing originating from natural and man-made water systems. The aim of this study was to describe the level of antimicrobial susceptibility of environmental spp. strains to preferred and recommended therapeutic agents to treat disease.

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Specific glycoproteins of the bovine subcommissural organ (SCO) were studied by means of various techniques: light and electron microscopy, immunoaffinity chromatography, electrophoresis and Western blotting. Use of lectins (Con A, WGA, PHA-E and -L, LCA) allowed to specify the synthesis and release of complex-type glycoproteins that bear high-mannose-carbohydrate chains in their precursor forms and probably triantennary carbohydrate chains in their mature forms. Antibodies raised against SCO extracts were characterized by means of various tests and used to purify specific compounds.

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To extend our previous immunochemical investigations in the chick embryo (Karoumi et al., 1990 b), we raised antibodies in the rabbit against crude extracts of the subcommissural organ (SCO) of the bovine. The antiserum labeled A99 was absorbed by crude brain extracts and its specificity was tested by different techniques.

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In the chick embryo, A74 immunoaffinity chromatography allowed to purify specific glycoproteins relevant to the SCO ventricular secretory process. The eluted fractions of the subcommissural organ (SCO), the cerebral hemispheres (CH) and the medulla oblongata (MO) were compared using the Concanavalin A (Con A) and wheat germ agglutinin (WGA) staining procedures after western-blotting. Analysis of the optical density of the reactive bands allowed to estimate the relative concentration of the various glycopeptides in the eluted fractions.

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Antibodies were raised in rabbit against crude subcommissural organ (SCO) extract of 19 day old chick embryos. After absorption with crude brain extract, the IgG fraction was purified by ion exchange chromatography. The specificity of the antibodies was controlled by immunostaining and by a competition test between lectins (Concanavalin A-Con A- and wheat germ agglutinin-WGA-) and antibodies (A74 IgG).

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