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Biomedical subjects

H Mouray

Publications and source records attributed to H Mouray.

15 recordsLinked to original sources
PubMed1992

[Rational prescription if protein evaluation in the diagnosis and follow up of protein-energy malnutrition].

In our countries, a good prescription of analysis would help to reduce hospital costs without modifying the efficiency of the diagnosis approach. In this work, the authors establish a bond between medicos and biologists by a good indication of protein check-up in the diagnosis and follow up of protein-energy malnutrition (PEM). After a discriminant analysis of all the results of protein check-up, two groups of markers are individualized depending on whether the PEM is accompanied or not by inflammatory complications. Finally, they recommend a systematic prescription of the useful group in case of inflammation associated with PEM, because infectious and parasitic diseases are almost constant among our malnourished infants.

Anthropometry↗
PubMed1979

Interactions in vitro and in vivo between rat serum protease inhibitors and anodal and cathodal rat trypsin and chymotrypsin.

Reaction mixtures of increasing amounts of the pancreatic homologous proteases, anodal and cathodal chymotrypsin and trypsin, respectively, and normal rat serum were analyzed by immunoelectrophoretic methods in order to determine their distribution on serum protease inhibitors. This paper concerns three proteins occurring in normal serum and capable of binding protease viz. alpha1-macroglobulin, alpha1-antitrypsin and alpha1-inhibitor 3. The distribution of the enzymes among these protease inhibitors differed significantly from one protease to another. The distribution of the proteases among the serum protease inhibitors following intravenous injection of 125I-labelled proteases corresponded to that in vitro. Complexes formed with alpha1-macroglobulin and alpha1-inhibitor 3 were quickly eliminated irrespective of the enzyme species used, whereas those formed with alpha1-antitrypsin persisted much longer in the circulation.

Animals↗
PubMed1979

A study of rabbit plasma progressive antithrombinic activity during acute phase inflammatory reaction and in experimental nephrotic syndrome.

1. The development of the progressive antithrombinic activity in rabbit plasma as a function of the level of the two alpha-macroglobulins in two experimental pathologies: acute phase inflammatory reaction and nephrotic syndrome, were studied. 2. In the first case, the antithrombinic activity is a result of the increased biosynthesis of plasmatic antithrombins: antithrombin III, alpha 1 antitrypsin and alpha macroglobulins. 3. In the nephrotic syndrome, this activity follows the increase in the alpha M levels, the other antithrombins having been massively eliminated from the circulation in the urine.

Animals↗
PubMed1978

Human alpha2-macroglobulin and its antitrypsic and antithrombin activities in serum and plasma.

alpha2-Macroglobulin level, trypsin protein esterase and progressive antithrombin activities were measured in normal and nephrotic sera and plasma. Trypsin protein esterase activity was proportional to the alpha2-macroglobulin concentration in serum and plasma from both normal and nephrotic patients. The results were different, however, with progressive antithrombin activity: in normal plasma, antithrombin III is the main thrombin inhibitor, then alpha2-macroglobulin and alpha1-antitrypsin, whereas in nephrotic syndrome patients, alpha2-macroglobulin is the main thrombin inhibitor.

Antithrombins↗
PubMed1978

The in vitro interactions of rat pancreatic elastase and normal and inflammatory ray serum.

The partition of labelled rat pancreatic elastase (EC 3.4.21.11) between the different protease inhibitors of rat plasma was studied at different levels of saturation of the inhibitors of rat plasma was studied at different levels of saturation of the inhibitor capacity of plasma with the enzyme. The reaction mixtures were analysed by immunoelectrophoretic methods utilizing specific antisera against the different inhibitors and by gel filtration on Sephadex G-200. Rat serum was shown to contain four elastase binding proteins. alpha 1-antitrypsin, alpha 1-macroglobulin and alpha 2-acute phase protein and alpha 1-inhibitor 3 which exhibits immunologic cross-reaction with human inter-alpha-trypsin inhibitor and is of similar molecular weight. With minute amounts of labelled elastase the partition among the binding protein was alpha 1-macroglobulin 60%, alpha 1-antitrypsin 24% and alpha 1-I3 16%. The 60% value of alpha 1-M bound radioactivity in normal serum corresponds to the sum of alpha 1-M and alpha 2-AP labelling in inflammatory serum.

Acute-Phase Proteins↗
PubMed1978

[Progressive antithrombin activity in rabbit plasma. Role of alpha macroglobulins].

Immunological methods associated with a kinetic study of blood coagulation allowed us to show the influence of the 2 rabbit alpha macroglobulins on the plasma progressive antithrombin activity. This study allowed the authors to discuss the participation of the alpha macroglobulins during the fibrinoformation and to think that these proteins have an immediate antithrombin activity.

Animals↗
PubMed1977

[Metabolism of alpha macroglobulins of rabbits: study of their half-life].

Rabbit alpha-1-M and alpha-2-M labelling was carried out in vitro with 131I and in vivo with 75-Seleno-methionine in order to determine the half-life of these proteins. alpha-2-M catabolism is faster than the alpha-1-M one. This result is the same when these proteins were obtained from a plasma of a rabbit exhibiting an inflammatory reaction though their half life was shorter.

Animals↗
PubMed1977

[Isolation of alpha-1-macroglobulin (alpha 1 M) and alpha-2-macroblogulin (alpha 2 M) from rabbit blood].

A purification process of rabbit alpha 1 M and alpha 2 M from plasma was described: first the platelets, the fibrinogen, the plasminogen and the low-density lipoproteins were eliminated; then alpha 1 M and alpha 2 M were purified by gel filtration on Sephadex G 200 and by chromatography on DEAE-cellulose. These purified materials were then isotopically labeled allowing the study of the proteins metabolism.

Animals↗
PubMed1976

Rat alpha2 acute-phase macroglobulin. Isolation and physicochemical properties.

1. Rat alpha2 acute-phase macroglobulin was isolated from turpentine-injected rats by Sephadex G-200 chromatography and ion-exchange chromatography on DEAE-cellulose. This method, since it does not include (NH4)2SO4 treatment, allows the study of the physicochemical as well as the biological properties of the molecule. 2. The purity of the preparation was demonstrated by ultracentrifugation, polyacrylamide-gel electrophoresis, fused "rocket" immunoelectrophoresis as well as double immunodiffusion. 3. The rat alpha2 acute-phase macroglobulin was characterized in terms of its main physical and chemical properties. Its isoelctric point was determined by isoelectrofocusing to be 4.55; s020,w was 18.4S and E1%/1cm at 278 nm was 6.8. The mol.wt. was determined by light-scattering to be 770000. 4. The amino acid content was compared with that of rat alpha1 macroglobulin and was found very similar. The carbohydrate composition of alpha2 acute-phase macroglobulin was determined to be: hexose, 4.25%; glucosamine, 3.4%; sialic acid, 2%; fucose, 0.2%. From these results it was concluded that alpha2 acute-phase macroglobulin, although a typical acute-phase reactant, possesses the characteristic physicochemical properties of alpha macroglobulins.

Amino Acids↗
PubMed1975

[Changes in the level of alpha1-macroglobulin in rats during Masugi nephritis].

Using chromatographic technique on "Sephadex G 200" associated to immunologic qualitative and quantitative techniques, the authors showed that the alpha1-macroglobulin is present in normal Rat urines. This protein is also present in urines obtained during the Masugi nephritis. The alpha1-macroglobulin concentration observed in the different urine samples is unrelated to the total proteinuria evolution. The results given allow us to discuss the mechanisms of the glomerular filtration.

Animals↗