[Effects of refeeding on serum immunoglobulin (IgA, IgG, IgM) concentrations in children with severe protein-energy malnutrition].

Background: Published studies on the serum immunoglobulin concentrations of patients with protein-energy malnutrition (PEM) have been contradictory. This report describes such a study in 21 Senegalese children.

Population And Methods: Twenty one Senegalese infants (mean age: 19 +/- 2 months) with severe PEM were included in the study.

[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.

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.

[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.

[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.