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Biomedical subjects

A Peltier

Publications and source records attributed to A Peltier.

At least 19 recordsLinked to original sources

[Consumption hypocomplementemia: comparative value of haemolytic and protein estimations of the components of the classical pathway (author's transl)].

Titrations of total complement (CH50) and of the different components of the classical pathway of the complement system in patients with supposed consumption hypocomplementemia, show that the complement depression involves in an order of decreasing severity hemolytic C4, hemolytic C2, total complement, hemolytic C1, protein C4 and protein C3. These results as well as correlative studies between these different parameters suggest that C4 is the most specific target of activited C1 esterase (C1s). They stress the interest of hemolytic titrations as well as the strong limitations of protein titrations.

Adolescent

[Serum and articular immune complexes detection by the antibody-dependent cytotoxicity inhibition reaction in inflammatory rheumatological conditions and connective tissue disorders (author's transl)].

Detection of circulating and intra-articular soluble immune complexes, has been done in 28 rheumatoid arthritis, 8 mixed connective tissue diseases and 8 other connective tissue diseases. The method used, is based on a competition reaction in the antibody dependent lymphocytotoxicity reaction (ADC). In rheumatoid arthritis serum immune complexes were detected in 75% of the seropositive cases and 66% of the seronegative ones. The mean level of complexes is higher in the former form of the disease. In a given patient, the concentration of immune complexes in joint fluid, is higher than in serum. Immune complexes were present in the serum of 75% of patients with mixed connective tissue disease, but, here, at a concentration lower than in rheumatoid arthritis and systemic lupus erythematosus. It is proposed that measurement of serum immune complexes, can also be an interesting parameter in the follow-up of the patients.

Antibody-Dependent Cell Cytotoxicity

Pseudo-clinical Fabry's disease without alpha galactosidase deficiency.

The authors describe two cases of clinical Fabry's disease. The first patient presents a deficiency of alpha galactosidase and a urinary excretion of ceramide trihexosides and dihexosides ; the second patient had a normal alpha galactosidase and normal excretion of urinary lipids. In this latter case the Km and the activity of the enzyme measured at different pH were similar to those of normal enzyme. The other lysosomal enzymes, beta galactosidase, beta glucosidase, hexosaminidases A and B, alpha fucosidase, arylsulfatases, phosphatase acids were also measured in patient 2 and all have normal activities. There is no urinary excretion of glycolipids or mucopolysaccharides. Yet this patient has an accumulation of material in his fibroblasts and renal cells. The authors also present a genetic study.

Adult

[Induction of N-acetyllactosamine synthetase activity in the mouse mammary gland by prolactin and placental lactogen hormone].

The authors show that the ovine prolactine promote induction of N. acetyl lactosamine synthetase in tissue culture of mammary glands of pregnant mice. A crude extract of human placenta has also a lactogenic activity as tested by the same method, but in this case the blank values are very high for large concentration of crude extract. The molecular forms of HCS are tested: the slow band has a lactogenic activity, the intermediate band has no activity and the rapid band seems to be inhibitory.

Animals

[Iso-hormones : molecular forms of human chorionic somatomammotropin (HCS) (author's transl)].

The chorionic somatomammotropin hormone extracted from the human placenta exists in several molecular forms: Analytical electrophoresis on polyacrylamide gel permits separation of a highly anodic migration form : form 1 and another form migrating slightly faster than albumin : form 2. These two forms are active as measured by radioactive immunological analysis, form 2 being about 25 times more active than form 1. The two forms are mutually interconvertible. The two forms may also be separated by filtration on Sephadex G-50. However, they do not differ in molecular weight, they have the same coefficient of apparent diffusion, measured by analytic ultracentrifugation. Glutaraldehyde and 8 M urea do not modify their electrophoretic or chromatographic behaviour. On the other hand, the two forms differ in their tertiary structure, with the modification depending on the greater or lesser degree of oxidation of the intra-chain disulfide groups. The two forms also exist in placental culture media and the incorporation of tritiated leucine occurs preferably in form 1, The physiological significance of the two hormone pools is not clarified.

Chromatography, Gel

Isohormones: molecular forms of the human chorionic somatomammotropic hormone.

The chorionic somatommaotropic hormone extracted from the human placenta exists in several molecular forms. Analytical electrophoresis in polyacrylamide gel permits separation of a highly anodic migration form, form 1, and another form migrating slightly faster than albumin, form 2. These two forms are active as measured by radioactive immunological analysis, form 2 being about 25 times more active than form 1. The two forms are mutually interconvertible. The two forms may also be separated by filtration on Sephadex G-50. However, they do not differ in molecular weight, they have the same coefficient of sedimentation and the same coefficient of apparent diffusion, measured by analytic ultracentrifugation. Glutaraldehyde and 8 M urea do not modify their electrophoretic or chromatographic behavior. On the hand, the two forms differ in their tertiary structure, with the modification depending on the greater or lesser degree of oxidation of the intra-chain disulfide groups. The two forms also exist in placental culture media and the incorporation of tritiated leucine occurs preferably in form 1. The physiological significance of the two hormone pools is not clarified.

Animals