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Biomedical subjects

M Weber

Publications and source records attributed to M Weber.

At least 793 records · Page 44Linked to original sources

[Association of Kaposi's sarcoma and Hodgkin's disease].

The authors report a new case of the association Hodgkin's disease and Kaposi's sarcoma. A woman of North African origin and suffering from mediastinal Hodgkin's disease developed, after the commencement of polychemotherapy with radiotherapy, Kaposi's cutaneous sarcoma, typical, clinically, histologically and by electron microscopy. In the light of this new case, the authors review 41 cases of the Hodgkin-Kaposi association found in the literature and discuss the inter-relations between Kaposi's sarcoma and diseases of the haemoreticular system, in particular carcinomas, immuno-depressive states (notably in association with renal transplants) and virus disorders (essentially herpes). It might be possible to incriminate in the aetiology of Kaposi's disease a carcinogenetic process of viral origin during a state of immuno-depression.

Adult↗

[Purification of alpha-amylase by affinity chromatography on cross-linked starch].

Affinity chromatography on cross-linked starch affords a simple and rapid procedure for alpha-amylases (EC 3.2.1.1.) purification. When starch is cross-linked in alkaline medium by epichlorhydrin in the conditions described, the insoluble polysaccharide obtained is able to retain specifically the alpha-amylase which is then eluted with 2M maltose solution. alpha-amylase can be obtained in a pure form with a 60% yield. The exoenzyme beta-amylase (EC 3.2.1.2) is not retained by the support and is eluted with other contaminant proteins. Therefore, this procedure allows the separation of the endo- and exoamylase activities.

Amylases↗

[Cutaneous manifestations due to acrylic resins used in printing].

In the plant of a large newspaper, the manufacture of printing plates using photopolymer acrylic resins, in the place of lead, resulted in a series of orthoergic and allergic manifestations in the workers. Chemical analysis resulted in the isolation of a tetraethylene glycol diacrylate, the harmful nature of which was proven by allergological studies. Its replacement by tetrathylene glycol dimethacrylate eliminated the problems seen (study based upon 300 allergological tests).

Acrylic Resins↗

Effect of antibody on interaction between vitamin B2 and riboflavin apoprotein.

1. Dissociation of riboflavin from flavoprotein and from the flavoprotein-antibody complex occurs under the same conditions. 2. The precipitated apoprotein-antibody complex retains 15% of the apoprotein capacity to bind riboflavin. After solubilization of the complex in 0.3 M-KCl or 1 M-urea, the binding of riboflavin amounts to 80 - 90% of its capacity. 3. The apoprotein modified by oxidation of 50% of tryptophan residues loses the ability to bind riboflavin but its immunological reactivity with the anti-flavoprotein antibody is similar to that of native apoprotein. The apoprotein with all tryptophan residues oxidized shows much lower immunoreactivity. 4. The obtained results suggest that in riboflavin flavoprotein the region around the riboflavin-binding site does not show the properties of an antigenic determinant.

Animals↗

The fine structure of the branched alpha-D-glucan from the blue-green alga Anacystis nidulans: comparison with other bacterial glycogens and phytoglycogen.

The fine structure of the glycogen from the blue-green alga Anacystis nidulans has been examined. After selective hydrolysis of all (1 yields 6)-alpha-D linkages by a bacterial isoamylase, the resulting mixture of linear chains was subjected to gel permeation chromatography. For purposes of comparison, the glycogens from Escherichia coli and Arthrobacter sp., amylopectin, phytoglycogen from sweet corn, and shell-fish glycogen were treated similarly. The profiles of the unit chains of A nidulans glycogen and phytoglycogen were closely similar. There was no close resemblance in the size distribution of unit chains for A. nidulans glycogen, other bacterial glycogens, and amylopectin.

Amylases↗

Regulation of binding properties of the nicotinic receptor protein by cholinergic ligands in membrane fragments from Torpedo marmorata.

Exposure of receptor-rich membrane fragments from Torpedo marmorata to carbamylcholine causes a slow (half-time of 5--10 min) and reversible change of properties of the cholinergic receptor protein manifested by a decrease of the initial rate of Naja nigricollis alpha-[3H]toxin binding in the presence of carbamylcholine. This change corresponds to a 5- to 20-fold increase of affinity for carbamylcholine. Other agonists, acetylcholine, phenyltrimethylammonium, show the same effect but not the antagonists d-tubocurarine and flaxedil. Decamethonium and hexamethonium show little, if any, agonistic effect in vitro on the same membrane fragments but cause the affinity change. This regulatory property can be lost after aging of the preparation of membrane fragments. Since the affinity increase progresses with a similar time course as the decrease of amplitude of the permeability response consecutive to agonist preincubation, it is proposed that, in the membrane at rest, the receptor protein is present under a state of low affinity for agonists and that the reversible stabilization by the agonists of a high affinity state corresponds to the "pharmacological desensitization" of the system as predicted by one of the models of Katz and Thesleff.

Acetylcholine↗

Proteinuria and distribution of fibrinogen split products in various forms of glomerulonephritis.

The microelectrophoresis on gradient gels allows differentiation between the different types of proteinuria in 1 h in a one-step procedure. Due to their different molecular weights and forms, fibrinogen split products are separated by this method. The determination of fibrinogen split products not only offers a possibility for dicrimination between the various forms of glomerulonephritis but also offers a possibility for following the course of the disease.

Electrophoresis, Polyacrylamide Gel↗

Method for diphenylhydantoin and phenobarbital assay by gas chromatography.

A rapid and easy method for determination of diphenylhydantoin and phenobarbital in plasma by gas liquid chromatography which provides monitoring of epileptic patients therapy is described. These drugs are extracted from plasma by partitioning between cholroform and buffered aqueous phase. The final extract is evaporated to dryness and the residue dissolved in an internal standard (methaqualone) solution. An amount of the final extract is injected tnto OV1 3% column at 230degreeC without previous derivative formation. The results are compared to those obtained by thin layer chromatography followed by colorimetry.

Buffers↗