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P Sicard

Publications and source records attributed to P Sicard.

8 recordsLinked to original sources

[Acute sphenoid sinusitis in adults].

Seven cases of acute sphenoid sinusitis were reviewed. Two happened after deep sea diving. Headache of variable location and fever were the most predominant presenting symptoms (5/7). Purulent discharge in the cavum was present in three. Correct diagnosis was delayed from six to twenty-four days after beginning of symptoms, when a neurologic deficit became apparent : mainly paralysis of the sixth and third cranial nerves. Computed axial tomography was the most useful radiologic procedure for demonstrating sinus opacification in every patient. Two patients died, three had complete recovery, one had persistent epileptic focus after brain abscess. Last patient had paraparesis and incontinence of urine after study of cerebrospinal fluid (C. S. F.) flow with methylene blue. Cannulation of the sphenoid sinus was performed in two patients and surgical drainage in three. Gram negative microorganisms and Staphylococcus aureus were isolated from the sphenoid sinus of only three patients. Blood cultures were negatives in every cases and C. S. F. in six. First choice antibiotics was an association of aminoglucosides and broad-spectrum penicillin in six cases. It always had to be changed.

Adult

[Physicochemical properties of an extracellular polysaccharide isolated from culture media of Bacillus amyloliquefaciens].

A new extracellular polysaccharide has been isolated by chromatography on anion exchanger of a fraction obtained from highly viscous culture media of Bacillus amyloliquefaciens. This polysaccharide is characterised by high molecular weight (1,000,000 dalton) and intrinsic viscosity (323 ml/g). It contains 24% neutral sugar (galactose and mannose 5:1), 35% glucuronic acid and 51.5% N-acetylhexosamines (N-actylglucosamine, N-acetylgalactosamine and N-acetylbacillosamine 6:9:1).

Bacillus

Large scale purification of hog renin. Physicochemical characterization.

Renin was purified from 47 kg of hog kidney to produce enough enzyme for enzymatic and physicochemical characterization. The procedure included extraction at pH 3.5 in the presence of protease inhibitors, two ammonium sulfate precipitations, ion exchange chromatography on Sepharose-hexamethylenediamino-pepstatin gel, gel filtration, and isoelectric focusing. Renin, 2.3 mg, with a specific activity of 1,100 GU/mg of protein was obtained with about 70,000-fold purification and 16% overall recovery. The purity criteria were: (1) a single band on sodium dodecyl sulfate (SDS)-gel electrophoresis, (2) same retardation factor on polyacrylamide gel electrophoresis for renin activity, protein and glycoprotein coloration. Renin was characterized by its stability at--20 degrees C, pH 6.5; its molecular weight on SDS-gel electrophoresis, 36,800; its relative mobility on polyacrylamide gel electrophoresis at pH 7.8; its isoelectric point, 5.15; its amino acid composition, which revealed that renin is a glycoprotein; and its Michaelis constant on tetradecapeptide substrate at pH 6.6, Km = 7.7 X 10(-6) M.

Amino Acids

Partial characterization of hog renin purified by affinity chromatography.

A method has been set up to purify renin on a large scale by affinity chromatography using Pepstatin, a potent inhibitor of renin, as a ligand. Pepstatin was covalently coupled to Sepharose via six different spacer 'arms'. The Sepharose-hexamethylenediamino-Pepstatin appeared to be the better derivative for renin purification even at a concentration as low as 160 nmol of Pepstatin/ml of moist gel. Renin was extracted from 100 kg of hog kidneys and semi-purified by ammonium sulfate precipitations and chromatography on DEAE-cellulose. The active fraction (48.5 g of proteins) was applied on a 500-ml affinity column. Renin was eluted in the starting buffer containing 6 M urea. Renin was purified 120-fold by the affinity chromatography step with a 79% recovery. Physico-chemical characterization of highly purified renin was performed. Isoelectrofocusing on a pH gradient from 3 to 6 showed a major peak with an isoelectric point (pI) of 4.95 and a minor peak (pI = 4.70). Polyacrylamide gel electrophoresis, pH 7.8, at different gel concentrations, showed a single peak of renin activity which was found in the major protein band. Molecular size estimated on agarose-acrylamide gel filtration was 40 000. All these physical parameters were similar before and after purification.

Animals

[Trombovar].

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Humans