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Biomedical subjects

P Roussel

Publications and source records attributed to P Roussel.

At least 127 records · Page 7Linked to original sources
PubMed1986

The major human urinary trypsin inhibitor is a proteoglycan.

The major urinary trypsin inhibitor (Mr 44 000), isolated from human urine, contains 35% carbohydrate. In addition to N-acetylglucosamine and neutral sugars (primarily mannose and galactose), the carbohydrate moiety contains hexuronic acid and N-acetylgalactosamine and corresponds to a glycosaminoglycan. This carbohydrate chain is an integral component of the inhibitor: it does not dissociate from the inhibitor when using dissociative conditions such as sodium dodecyl sulfate, guanidinium chloride, or by increasing ionic strength or mixing with cetylpyridinium chloride. This glycosaminoglycan chain is sensitive to chondroitinase ABC or testicular hyaluronidase digestion and corresponds to slightly sulfated chondroitin 4-sulfate or 6-sulfate. After treatment by these enzymes, the urinary inhibitor has a lower molecular mass (Mr 26 000) but still inhibits trypsin.

Amino Acids↗
PubMed1986

Structure of sialyloligosaccharides isolated from bonnet monkey (Macaca radiata) cervical mucus glycoproteins exhibiting multiple blood group activities.

Mucin glycoproteins purified from cervical epithelial secretion of the bonnet monkey (Macaca radiata) exhibit multiple blood group activities. Alkaline borohydride reductive cleavage resulted in a mixture of neutral and acidic oligosaccharide-alditols. By high-performance liquid chromatography, seven oligosaccharides (A-4-1 to A-4-7) have been purified from the monosialyloligosaccharide fraction (A-4). Based on the results of 500-MHz 1H NMR spectroscopy, in conjunction with sugar analysis and immunological assays, we propose the following structures for these oligosaccharides. (formula: see text) These structures imply that either the A, B, or H determinant may be found in combination with the Cad/Sda determinant; the oligosaccharides identified, together, account for the blood group activities exhibited by the cervical mucus.

Animals↗
PubMed1986

The high lipid content of respiratory mucins in cystic fibrosis is related to infection.

Seven human bronchial mucins secreted by patients suffering from chronic bronchitis or from cystic fibrosis were prepared by exclusion from a Sepharose CL-2B column in 6 M guanidinium chloride. Their behaviour in CsBr density gradient centrifugation was compared. The mucin fractions were associated with peptides and lipids, the abundance of which decreases with the buoyant density. The lipid content of the mucin fractions appears to be related to the infectious character of the bronchial secretion and seems to be independent of cystic fibrosis. The content of fatty acids remaining after delipidation of mucin fractions from patients with chronic bronchitis or with cystic fibrosis also appears to be related more to the purulent character of the sputum than to cystic fibrosis or chronic bronchitis.

Bronchi↗
PubMed1986

Reducing the artifacts produced by impure antisera in immunoblots of low-molecular-mass proteins in urine.

Immunoblots of several urinary low-molecular-mass proteins can be very useful in investigations of pathological proteinuria. However, use of certain commercial antisera in such procedures leads to artifacts corresponding to nonspecific bands; e.g., immunoglobulins from nonimmunized rabbit serum may bind to human urinary proteins, and this binding is not inhibited by Triton X-100. We have developed a procedure to improve the specificity of detection of urinary low-Mr proteins separated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, by immunoblotting with commercial antisera: we treat the protein blot with a mixture of mercaptoethanol and sodium dodecyl sulfate before incubation with the first antiserum. This allows direct use of commercial antisera without prior absorption of contaminating antibodies.

Alpha-Globulins↗
PubMed1986

High performance liquid chromatographic determination of paracetamol in human serum.

A method has been developed for the determination of acetaminophen in human serum. Samples are extracted with ethyl acetate. Beta-hydroxyethyl theophylline is used as internal standard. The solvent is evaporated under nitrogen and the residue is analyzed by high-performance liquid chromatography on Lichrosorb RP 18. Extraction efficiency, linearity and assay precision have been determined. The method is rapid and can be easily applied to determine the plasma level of patient having taken overdose of paracetamol.

Acetaminophen↗
PubMed1985

Estimating viral concentrations: a reliable computation method programmed on a pocket calculator.

A method has been developed, based on the Newton-Raphson iterative procedure, for calculating the concentration of viral suspensions from the dose-response data yielded by the cytopathic effect assays. The computation method provides the maximum likelihood estimate with its 95% approximated confidence limits, and determines the value of chi 2 for testing the goodness of the fit. A program for a Hewlett-Packard 41C calculator is presented which is suitable to most experimental situations.

Computers↗
PubMed1984

Further characterization, by a combined high-performance liquid chromatography/1H-NMR approach, of the heterogeneity displayed by the neutral carbohydrate chains of human bronchial mucins.

From bronchial mucins of cystic fibrosis patients with blood group O, the carbohydrate chains were released in the form of oligosaccharide-alditols by alkaline borohydride treatment. Application of high-performance liquid chromatography directly on the pool of neutral oligosaccharides afforded 23 fractions. Twenty oligosaccharide structures were characterized by employing 500-MHz 1H-NMR spectroscopy in conjunction with sugar analysis. Thirteen among these had been revealed before to occur in human bronchial mucins [Van Halbeek, H., Dorland, L., Vliegenthart, J. F. G., Hull, W. E., Lamblin, G., Lhermitte, M., Boersma, A., and Roussel, P. (1982) Eur. J. Biochem. 127, 7-20], when paper-chromatographic fractionation of this pool of neutral oligosaccharides was employed. High-performance liquid chromatography enabled to obtain another seven pentasaccharide and hexasaccharide alditols; the largest-size representatives are: (Formula see text). Thereby, this approach afforded deeper insight into the structural heterogeneity displayed by the carbohydrate chains of bronchial mucins.

Bronchi↗
PubMed1984

Primary structure determination of five sialylated oligosaccharides derived from bronchial mucus glycoproteins of patients suffering from cystic fibrosis. The occurrence of the NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)] GlcNAc beta(1----.) structural element revealed by 500-MHz 1H NMR spectroscopy.

The structure of sialylated carbohydrate units of bronchial mucins obtained from cystic fibrosis patients was investigated by 500-MHz 1H NMR spectroscopy in conjunction with sugar analysis. After subjecting the mucins to alkaline borohydride degradation, sialylated oligosaccharide-alditols were isolated by anion-exchange chromatography and fractionated by high performance liquid chromatography. Five compounds could be obtained in a rather pure state; their structures were established as the following: A-1, NeuAc alpha(2----3)Gal beta(1----4) [Fuc alpha(1----3)]GlcNAc beta(1----3)Gal-NAc-ol; A-2, NeuAc alpha(2----3)Gal beta(1----4)GlcNAc beta(1----6)-[GlcNAc beta (1----3)]GalNAc-o1; A-3, NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1; A-4, NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)]Glc-NAc NAc beta(1----6)[GlcNAc beta(1----3)]GalNAc-o1; A-6,NeuAc alpha-(2----3) Gal beta(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----6)[Gal beta-(1----4) GlcNAc beta(1----3)]GalNAc-o1. The simultaneous presence of sialic acid in alpha(2----3)-linkage to Gal and fucose in alpha(1----3)-linkage to GlcNAc of the same N-acetyllactosamine unit could be adequately proved by high resolution 1H NMR spectroscopy. This sequence constitutes a novel structural element for mucins.

Bronchi↗
PubMed1984

Complex structure of human bronchial mucus glycoprotein.

Human bronchial mucus glycoproteins or mucins were isolated from the sputum of two patients by a method avoiding reducing agents and involving water extraction and gel filtration on Sepharose CL-2B in 6 M guanidinium chloride. The chemical analysis indicated approximately 25-40% lipid. The amino acid and carbohydrate analysis differ quantitatively from that of mucins purified after prior reduction of mucus. These fractions also have a higher proportion of aspartic and glutamic acids than that of the mucins from reduced sputum. These mucins are still contaminated by small amounts of peptides but do not seem to contain disulfide-attached cross-linking protein. Human bronchial mucins have a strong tendency to form aggregates except in 6 M guanidinium chloride. Electron microscopy performed with various procedures indicates the presence of both micelles and flexible threads measuring 200-1000 nm. Delipidation removes most of the micellar forms. Thereafter mucins appear mainly as polydisperse flexible extended threads and also as aggregates. These features of bronchial mucins do not fit with the generally accepted idea of mucin subunits linked by disulfide bridges (unless they are linked end to end) and alternatively favour a model where mucin molecules behave like filaments that could easily aggregate according to the solvent system (mucin concentration, absence of dissociating conditions).

Amino Acids↗
PubMed1983

Activation of bronchial mucin proteolysis by 4-aminophenylmercuric acetate and disulphide bond reducing agents.

High molecular weight bronchial glycoproteins, as nearly native as possible, were treated with either 2-mercaptoethanol or 4-aminophenylmercuric acetate (APMA): analytical electrophoresis revealed that a decrease in molecular weight of glycoproteins coincided with the disappearance of some proteins associated with high molecular weight bronchial glycoproteins. These modifications were not observed if high molecular weight bronchial glycoproteins were incubated with paramethylsulphonyl fluoride and EDTA, two synthetic protease-inhibitors, prior to 2-mercaptoethanol or APMA action. These data suggest that protease-antiprotease complexes are associated with bronchial mucins and that reducing agents or APMA activate proteases.

Bronchi↗
PubMed1983

Possible amino acid repetitive sequences in the proline-rich glycoprotein of human parotid saliva.

The amino acid sequence of the proline-rich glycoprotein from human parotid saliva was studied using different preparations: native glycoprotein, tryptic glycopeptides, and their chemically deglycosylated homologous derivatives. The results indicate very similar structural features of the proline-rich glycoprotein and the tryptic glycopeptides and suggest that the peptide backbone of the glycoprotein comprises several repetitive domains containing one carbohydrate-peptide linkage and a proline-rich sequence. These data are in fair agreement with a preceding circular dichroism study (Aubert, J.P., Porchet, N., Boersma, A., Loucheux-Lefevbre, M.H. and Degand, P. (1982) Biochim. Biophys. Acta 704, 361-365).

Amino Acid Sequence↗