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Biomedical subjects

R Julien

Publications and source records attributed to R Julien.

At least 127 records · Page 7Linked to original sources

[Micromethod of diazepam determination in the blood by gas-liquid chromatography. Application in neonatal pharmacology].

We propose a micromethod of diazepam determination on 0,1 ml of whole blood. The extraction is made with n-heptane for the isolation of diazepam in presence of principal metabolites. For the usual concentrations, the precision is about 3 per cent; at the detection limite, 0,05 mug/ml, it is about 20 per cent. With this method we studied the pharmacokinetics of diazepam in neonate with convulsive diseases in comparison with electroencephalogram.

Chromatography, Gas↗

[Cellular distribution of elongation factor EF1 in wheat germ].

Cellular distribution of elongation factors (EF1) from imbibed then redessicated wheat embryos is determined after purification and analytical gel electrophoresis of soluble and ribosome-bound factors. Two heavy forms (EF1 H, mol. wt, 250 000) are found in cytosol while ribosome-bound factors contain a light form (EF1L, mol. wt, 45 000) with the greatest activity and a heavy form (mol. wt, 160 000) which might well be an intermediary in the recycling of ribosomal factor EF1L to soluble factor EF1H.

Chromatography↗

Further characterization of bovine pancreatic lipase.

1. The amino acid composition of bovine pancreatic lipase is very similar to that of porcine lipase. 2. Bovine lipase possesses a residue of lysine at the N-terminal position and a half cystine or a cysteine at the C-terminal position. 3. Bovine lipase contains two free sulfhydryl groups of different reactivities to 5, 5'-dithiobis-(2-nitrobenzoic) acid. One of these groups is buried in the native conformation of the enzyme and is fully titrated in 1.5 M urea when reaction is performed in the presense of 1 mM EDTA.

Amino Acids↗

Ovine pancreatic lipase : purification and some properties.

Lipase has been isolated from sheep pancreas. The lipoprotein complex formed in pancreas homogenates by the enzyme and endogenous lipids is split by treatment with acetone. Lipase is further purified by ion-exchange chromatography and gel filtration. The molecular weight and the amino-acid composition of ovine lipase are very similar to that of the porcine and bovine enzymes. As previously found in bovine lipase, no carbohydrate is covalently bound to the polypeptide chain which has a N-terminal residue of lysine. The study of the catalytic properties of ovine pancreatic lipase indicates that the enzyme is fully activated by colipase from various species in the presence of conjugated bile salt micellar solutions.

Amino Acids↗

Studies on the effect of bile salt and colipase on enzymatic lipolysis. Improved method for the determination of pancreatic lipase and colipase.

The rate of hydrolysis of long chain triglycerides by pure bovine pancreatic lipase has been determined in the presence of variable amounts of bile salts and colipase. Cofactor-free lipase is strongly inhibited by sodium taurodesoxycholate and by mixed bovine bile salts at concentrations higher than the critical micellar concentration. Bile salt inhibited lipase is reactivated by the addition of bovine colipase. Gel filtration of pancreatic juice from several species (Cow, dog, pig) on Sephadex G 100 allows the separation of lipase from colipase. It is found that the enzyme catalyzed hydrolysis of long chain triglycerides by pancreatic lipase from one species is activated by the addition of colipase from other species. Studies on the activation of pancreatic lipase by colipase in the presence of bile salts allowed the re-evaluation of optimal conditions for the determination of lipase and the development of a procedure to assay colipase.

Animals↗

Isolation and partial characterization of bovine pancreatic colipase.

Three molecular forms of colipase (colipases A, B and C) with the same specific activity have been isolated from an acid extract of bovine pancreas. Purification includes ammonium sulfate precipitation, ethanol treatment, chromatography on SP-Sephadex, chromatography on DEAE-cellulose and chromatography on QAE-Sephadex. The most basic form of bovine colipase (colipase A) has a molecular weight of 11,000-12,000 daltons and contains 104 residues. Its aminoacid composition is very similar to that of the intact form of porcine colipase isolated by Borgström et al. Colipases from both species have the same N-terminal residue (valine). It is likely that bovine colipases B and C represent partially degraded forms of colipase A. Their cofactor activity, however, is the same.

Amino Acids↗

[Thermovision applied to relaxation].

Dynamic telethermography (thermovision) affords at distance picking up on a T.V. screen (black and white or color) of the thermal body map. Its use in relaxation (autogenic training) enabled us to study in their overall, the thermal modifications observed during the relaxation. We have been able to find changes occurring in the release of heat at the front of the neck and at the inner corner of the eye socket; up to now, this had been unnoticed. Finally, it has allowed a dynamic work: the progression in heat release at the extremities of the limbs, at the thorax and the abdomen level was subject to an accurate and detailed study which leads to future prospects of interest by showing vascular exchanges, the thermal changes of which being only reflecting them.

Autogenic Training↗