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Biomedical subjects

P Roussel

Publications and source records attributed to P Roussel.

At least 163 records · Page 9Linked to original sources
PubMed1979

Evidence for heterogeneous or incomplete immunoglobulins in oligoclonal CSF studied by electroimmunofixation.

10 oligoclonal CSF have been studied by electroimmunofixation techniques on Cellogel RS. The gammaglobulin bands are either homogeneous or heterogeneous. The heterogeneous bands migrate preferentially in the cathodic part of the gamma zone. The light chain type of many homogeneous bands is lambda. Some oligoclonal bands may be composed of free homogeneous light chains. The free lambda chains have a more anodic migration than the free kappa chains. Furthermore, our results suggest the presence of free heavy chains in some instances.

Humans↗
PubMed1979

Chemical and physical properties of human bronchial mucus glycoproteins.

Human bronchial mucus glycoproteins of different chemical types were isolated by Ecteola and gel exclusion chromatography. Chemical analysis indicated polydispersity with regard to content of sulfate and sialic acid. No blood group A, B or H activity was found in these glycoproteins. Compositions are reported for amino acid and sugar residues for several fractions obtained from both cystic fibrotic and chronic bronchitic mucus. It is noteworthy that glycoproteins extracted from a single subject contain molecules with different acid groups as well as significant differences in carbohydrate chain length.

Amino Acids↗
PubMed1979

[Adaptation to Gemsaec centrigugal analyser of a method of turbidimetric estimation of amylase (author's transl)].

Hydrolysis of a solution of amylopectin by serum or urinary amylase leads to a reduction of the turbidity of this solution, observed at 340 nm. Adapted to centrifugal analysis, this method permits 15 estimations in 3 minutes with a serial reproducibility of 2.7 per cent, and a daily reproducibility of 6 per cent. The correlation with a nephelemetric method of estimation gives r = 0,969, with an enzyme method r = 0,957 and with an amyloclastic method, r = 0,919.

Amylases↗
PubMed1977

[Heterogeneity of carbohydrate chains of acidic bronchial mucin isolated from the spatum of two subjects with chronic bronchitis].

Acidic glycoproteins having blood group H activity were isolated from the sputum of two patients suffering from chronic bronchitis by reduction of the fibrillar mucus, chromatography on ECTEOLA-cellulose and gel filtration on Sepharose 4-B. These glycoproteins were degraded with alkaline borohydride and the degradation products were fractionated by chromatography on ionexchange resins and by gel filtration. The carbohydrate chains have a wide heterogeneity with regard to acidity and molecular size. Therefore carbohydrate chain heterogeneity which was already observed for bronchial glycoproteins isolated from a patient suffering from cystic fibrosis is not specific for cystic fibrosis.

Amino Acids↗
PubMed1977

Affinity of bronchial secretion glycoproteins and cells of human bronchial mucosa for Ricinus communis lectins.

The coupling of Ricinus communis lectins to Sephadex G 25 was used in order to study mucins and other glycoproteins from human bronchial secretion. The major part of human bronchial mucins and other glycoproteins such as immunoglobulins A, bronchotransferrin and alpha1-antichymotrypsin were isolated by this procedure. A parallel study of human bronchial mucosa was achieved with peroxidase labeled Ricinus communis lectins; this study characterized goblet cells and mucous cells which contain mucins, and serous cells which are involved in the synthesis or the secretion of the other glycoproteins.

Amino Acids↗
PubMed1977

Limulus polyphemus lectin sites in human bronchial mucosa.

The lectin from Limulus polyphemus (limulin) has an affinity for glycoproteins containing N-glycolyl or N-acetylneuraminic residues. By using a peroxidase labeled limulin on human bronchial mucosa sections, it has been possible to demonstrate selectively a diffuse staining within the apical part of the epithelial goblet cells. Whereas, in the submucosal glands serous cells, the labeling appears as small granules localized either at the apical pole or in the whole cytoplasm. In our experimental conditions the labeled limulin has no affinity for mucous cells that are known to contain sialic acid residues.

Arthropods↗
PubMed1977

[Pancreatico-peritoneal fistula in the newborn infant revealed by a hemorrhagic ascites].

Chronic haemorrhagic ascites in an infant is reported. After much hesitation without a definite diagnosis the first laparotomy was carried out and the estimation of amylase, lipase and proteolytic enzyme activities in the ascitic fluid suggested a pancreatic origin for the ascites. This was conformed at a second laparotomy when the condition was correted. This emphasises the importance of the estimation of pancreatic enzymes in unexplained ascites in children.

Ascites↗
PubMed1976

[Studies on the activities of peptidases from human leucocytes, and human and guinea pig alveolar macrophages (author's transl)].

Peptidases activities were compared in human leucocytes, guinea pig and human alveolar macrophages. Seversl endo- and exopeptides were characterized; some of them were active at acid pH and others at neutral and alkaline pH. Leucocytes and alveolar macrophages had proteolygic activity for hemoglobin, fibrinogen, collagen and elastin. Using synthetic substrates, several enzymes were characterized: arylamidase, aminopeptidase, carboxypeptidases A and B and cathepsins A and C. The enzymatic activities were much higher in alveolar macrophages than in leucocytes.

Animals↗
PubMed1976

Properties of human neutral bronchial mucins after modification of the peptide or the carbohydrate moieties.

Trypsin and pronase treatment of purified human neutral bronchial mucins released small fragments from the C-terminal end of these molecules and resulted in slight increases in their sedimentation coefficient presumably reflecting conformational changes. The antigenic determinant of neutral bronchial mucins which appears to be located on this C-terminal fragment is destroyed by pronase or by treatments such as periodate oxidation or galactose oxidase-bromine oxidation which modify the carbohydrate moieties. Thus, both amino acid and carbohydrate residues are involved in the structure of the antigenic determinant.

Amino Acid Sequence↗
PubMed1975

[Endo beta-N-acetylglucosaminidase in human liver].

Endo beta-N-acetylglucosaminidase activity was found in a alpha-L-fucosidase preparation purified from human liver homogenates, using glycopeptides from human parotid glycoprotein as a substrate. An oligosaccharide was purified and after reduction N-acetylglucosaminitol was shown by paper chromatography. Thus, the specificity and the significance of this endoglycosidase in glycoprotein catabolism are discussed.

Acetylglucosamine↗
PubMed1975

[Comparative studies of the acid hydrolases of human leucocytes and human and guinea pig alveolar macrophages. I. Study of the activities of glycosidases, arylsulfatase and acid phosphatase (author's transl)].

Acid hydrolase activities were compared in human leucocytes, guinea pig and human alveolar macrophages. Several enzymes were characterized: N-acetyl-beta-D-glucosaminidase, N-acetyl-alpha- and beta-D-galactosaminidase, alpha and beta-D-galactosidase, alpha-D-mannosidase, alpha-L-fucosidase, beta-D-glucuronidase, neuraminidase, acid phosphatase and arylsulfatase. The enzymatic activities were lower in leucocytes than in alveolar macrophages, higher in human macrophages than in guinea pig macrophages, except for beta-D-glucuronidase, acid phosphatase and arylsulfatase activities.

Acetylglucosaminidase↗