Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0272170 (SDS)
 50,377 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Secreted human bronchial mucins, directly collected from macroscopically healthy bronchial mucosa, were prepared in the presence of six proteinase inhibitors, and analysed by electron microscopy. These mucins were similar in length distribution to molecules prepared from sputum [Slayter, Lamblin, Le Treut, Galabert, Houdret, Degand & Roussel (1984) Eur. J. Biochem. 142, 209-218], although they were a little longer, their lengths ranging up to about 1,650 nm. This length corresponds to an extended mucin peptide of about 450 kDa. In order to compare these peptide lengths with the molecular size of biosynthetic precursors, an antiserum raised against trifluoromethanesulphonic acid-treated highly glycosylated regions of human bronchial mucins was used to isolate mucin precursors synthesized in explants of human bronchial mucosa during pulse-labelling with [3H]threonine or [3H]glucosamine. A main precursor labelled with [3H]threonine and with an apparent molecular mass of about 400 kDa was detected by fluorography following SDS/polyacrylamide-gel electrophoresis. This band was observed as early as 20 min; it was more intense after a 40 min chase and had disappeared after a chase period of 280 min in unlabelled medium, presumably owing to glycosylation. Much fainter bands at about 200 kDa and between 200 and 400 kDa, also labelled with [3H]threonine, were observed mainly after a 40 min chase and had disappeared after a 280 min chase. None of these bands was labelled with [3H]glucosamine, nor did they disappear after multiple treatments with immobilized lectins. After a 280 min chase, [3H]threonine-labelled material appeared in the stacking gel, which also contained [3H]glucosamine label. The results indicate that the 200-400 kDa species are mucin precursors, whose size is comparable with that obtained by electron microscopy for respiratory mucins collected directly from the macroscopically healthy bronchial mucosa.
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PMID:Peptides of human bronchial mucus glycoproteins. Size determination by electron microscopy and by biosynthetic experiments. 244 63

Considerable amounts (200 units/ml) of neuraminidase activity were detected in middle ear effusion of children (age 1 month-10 years) and its presence was highly correlated with the presence of Streptococcus pneumoniae. When isolates of this organism are cultured, neuraminidase activity appears in the growth medium during the exponential phase of growth. In order to study the role of this enzyme in the pathology of otitis media we have developed a method for its purification. The enzyme was purified over 5,800-fold by removing the organism and passing the culture broth through a series of affinity and ion-exchange columns. The overall yield was 2 mg enzyme protein and the final specific activity was 1.8 X 10(6) units/mg protein. A molecular weight of 65,000 was estimated by SDS-PAGE and gel filtration chromatography. The Stokes radius of neuraminidase was calculated to be 32 A, its isoelectric point was 7.2, and its pH optimum was 6.0. In terms of specificity, the enzyme catalyzed the hydrolysis of sialic acid linkages in mucin, glycoproteins, and gangliosides: bovine submaxillary mucin supported the highest catalytic efficiency, and alpha-1-antitrypsin the lowest. Neuraminidase acted on at least three linkage classes of substrates, alpha-2,6 and alpha-2,3 linkages of N-acetylneuraminic acid to galactose, and alpha-2,6 linkages to N-acetyl-galactosamine.
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PMID:Purification and properties of Streptococcus pneumoniae neuraminidase. 254 12

Monoclonal antibody KP16D3 was produced by immunizing mice with monkey bronchoalveolar lavage. KP16D3 revealed the immunohistochemical reactivity in the cytoplasm of some nonciliated bronchiolar epithelial cells and type II pneumocytes and thereby recognized specifically a protein with an apparent molecular weight of 60 kD with the use of Western blotting and immunoaffinity column chromatography followed by SDS-PAGE. Examination of 76 primary and 4 metastatic lung carcinomas in primary lung carcinoma KP16D3 showed immunohistochemical positivity only to mucin-nonproducing papillary adenocarcinoma (27/28) and bronchioloalveolar carcinoma (2/2), except for one case of large cell carcinoma. All other primary lung carcinomas such as squamous cell carcinoma, acinar adenocarcinoma, and small cell carcinoma had negative results. From these findings, KP16D3 seems to be an effective immunohistochemical marker of mucin-nonproducing papillary adenocarcinoma and bronchioloalveolar carcinoma of the lung and it appears to be useful to investigate both the histogenesis and functional expression of primary lung adenocarcinoma.
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PMID:Immunohistochemical study of lung adenocarcinoma using monoclonal antibody for 60-kilodalton antigen in type II pneumocytes and nonciliated bronchiolar epithelial cells. Comparison with two antisurfactant apoprotein antibodies. 254 7

The current work was undertaken to purify porins of Salmonella typhi, which are outer membrane proteins (OMPs) that induce protection in mice against challenge with the bacteria in mucin. OMPs, isolated with a non-ionic detergent, had a 4% contamination with LPS (endotoxin) and molecular sizes ranging from 17 to 70 KDa. Porins (Mw 38-41 KDa) were isolated from OMPs preparative SDS-PAGE. Anti-porins antisera were raised in rabbits and specific IgG was purified, which was coupled to Sepharose-CNBr. This immunosorbent was used to purify LPS-free porins.
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PMID:[Elaboration of an immunosorbent for the purification of porins from Salmonella typhi 9, 12, Vi:d]. 256 34

Purified intestinal mucins from eight normal subjects (N) and six patients with cystic fibrosis (CF) were compared for: (1) their content of free thiol groups (-SH) and disulphide bonds (S-S), (2) their immunoreactivity in a specific enzyme-linked immunoassay (ELISA) for the disulphide-bound 118,000 Mr glycoprotein and (3) their content of 118 kDa glycoprotein. Results showed considerable variability in the S-S/-SH content of individual mucin preparations but no differences were observed between N and CF samples. In the ELISA, all mucins were found to have identical antigenic determinants with the same affinity for the anti-118 kDa glycoprotein antibody but marked differences (ranging from 0.2 to 120,000 ng mucin) were observed in their relative immunoreactivities, indicating variable numbers of antigenic determinants. In general, CF mucins appeared to react more strongly in the immunoassay than N mucins. By SDS/polyacrylamide-gel electrophoresis under reducing conditions and densitometric analysis of Coomassie blue-stained gels, differences (up to six-fold) were also detected in the amount of 118 kDa glycoprotein in individual mucin preparations. However, this did not appear to be the cause of the variations in mucin immunoreactivity because not all strongly antigenic mucins contained large amounts of 118 kDa glycoprotein. Thus, accessibility of the 118 kDa glycoprotein to the antibody or the number of functional antigenic determinants within the 118 kDa glycoprotein may vary among different mucin preparations. The greater antigenicity of CF mucins may therefore reflect changes in their macromolecular conformation or in their 118 kDa glycoprotein.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Disulphide bonds and the 118,000 Mr glycoprotein of human intestinal mucin. 264 11

Bronchial mucin peptide chains were obtained by performing a two-step chemical deglycosylation of the highly glycosylated regions (or glycopeptides) which are the most characteristic part of bronchial mucins. The deglycosylated preparation was used to prepare an antiserum directed against mucin peptide epitopes. This antiserum reacted with the area containing rough endoplasmic reticulum of goblet cells and of mucous gland of human bronchial mucosa but not with secretory vesicles. The antiserum was used for immunoprecipitation of radiolabelled mucin precursors in pulse-chase experiments with explants of human bronchial mucosa. SDS-polyacrylamide gel electrophoresis followed by fluorography revealed precursors with a molecular mass in the range of 200 to 400 kDa as early as after 10 min pulse labeling with [3H]threonine. These results suggest that the mucin polydispersity previously visualized by electron microscopy may be explained by the synthesis of several respiratory mucin peptide precursors with different molecular sizes and/or that precursors with different amounts of carbohydrate are rapidly formed.
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PMID:Identification of human tracheo-bronchial mucin precursors. 270 84

Milk fat globules are secreted by envelopment in plasma membrane of the lactating cell. SDS-gel electrophoresis of proteins from this membrane has revealed differences between milk donors in two mucin-like glycoproteins. One of these glycoproteins resolves in 3% acrylamide stacking gel and the other in 4% running gel. The proteins vary in number of bands (one or two) and band mobilities. This polymorphism arises, at least in part, from expression of hypervariable genes. In this study, gel electrophoretic evidence of similar polymorphism in glycoproteins from cow, chimpanzee, horse and human milks is presented. In distinction to the other species, the cow expressed only one of these proteins which was detected in the running gel at Mr 180,000 to 200,000. The electrophoresis pattern for this protein from six cows was highly varied with respect to number (one or two) and position of bands. Peanut agglutinin, wheat germ agglutinin and concanavalin A all were bound specifically by bands of the bovine glycoprotein. Binding of concanavalin A distinguishes the bovine protein from the two human glycoproteins. Further studies of species differences should help shed light on the evolution of these unique glycoproteins and their possible functions in mother and young.
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PMID:Differences between individuals in high-molecular weight glycoproteins from mammary epithelia of several species. 271 10

The cell-bound sialidase of Actinomyces viscosus DSM 43798 was solubilized by mechanical cell disruption and lysozyme treatment. The enzyme was enriched 30,000-fold by cation-exchange chromatography, gel-filtration, and FPLC ion-exchange chromatography, thus obtaining 10 micrograms sialidase protein from 26 g wet cells with a specific activity of 680 U/mg protein. Since sialidase activity was also found in the culture medium, this enzyme was isolated as well, requiring the additional application of FPLC gel-filtration. Both sialidase preparations were apparently homogenous on SDS-PAGE and have similar properties. The substrate specificity of the A. viscosus sialidase was tested with 16 sialoglycoconjugates: The enzyme showed a higher activity with serum glycoproteins than with gangliosides, mucins or sialyllactoses. 4-O-Acetylated N-acetylneuraminic acid was not cleaved from equine submandibular gland mucins or serum glycoproteins in contrast to N-acetyl- and N-glycoloylneuraminic acid. 9-O-Acetyl-N-acetylneuraminic acid was released from bovine submandibular gland mucin, as confirmed by TLC. The sialidase hydrolyses alpha(2----6)-linkages more rapidly than alpha(2----8)- and alpha(2----3)-bonds. Cations, except Hg2+, or chelating agents have no influence on enzyme activity. The sialidase has a relatively high molecular mass of 150 kDa, but consists of only one unit. The enzyme is labile towards freezing and thawing, but can be stored at 4 degrees C in 0.1 M acetate buffer, pH 5.
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PMID:Properties of sialidase isolated from Actinomyces viscosus DSM 43798. 274 53

To clarify the etiology of intrahepatic calculus formation, we examined the components of hepatic bile, particularly glycoprotein, in 20 controls and 10 patients with intrahepatic calculi. The results obtained were summarized as follows: 1) The yield of delipidized bile powder was approximately 2.5 times higher in intrahepatic calculosis than in control. Quantitative analysis revealed that protein and neutral sugar were significantly increased in intrahepatic calculosis as compared with those in control. In SDS-PAGE of the powder, both intrahepatic calculosis and control groups demonstrated almost similar patterns except for difference in stainability between groups. This indicates that glycoprotein, that had been already present in control bile, was markedly increased in hepatic bile in intrahepatic calculosis. SDS-PAGE also demonstrated a thick and deep-stained band near the starting point only in intrahepatic calculosis. 2) Chromatography obtained from gel filtration on Sepharose CL-6B revealed 2 large peaks, one in void volume (macromolecular) and the other in total volume (micromolecular) region. In chemical analysis, macromolecular fraction in intrahepatic calculosis was rich in galactosamine, fucose and sialic acid, and characterized by prominent serine and threonine, which indicated that it was composed mainly of mucin type sialoglycoprotein. The micromolecular fraction in both groups were rich in aspartic acid and mannose, which indicated that they were composed mainly of serum type glycoprotein.
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PMID:[Role of bile glycoprotein in intrahepatic calculus formation]. 274 7

Mucin from xenografts of LS174T human colon cancer cells was treated with anhydrous HF for 1 h at 0 degree C to give a product (HFA) with over 80% of the glucosamine and hexose removed, but retaining some galactosamine, and for 3 h at room temperature to give a product (HFB) devoid of carbohydrate. Rabbit antibodies against HFA bound to HFA much more than to HFB, and bound to native mucin to an intermediate extent. Antibodies to HFB bound to HFB more than to HFA, and did not bind to native mucin. Both HFA and native mucin bound a number of lectins, but HFB did not. By SDS/polyacrylamide-gel electrophoresis and size-exclusion h.p.l.c., native mucin and HFA are of apparent molecular mass greater than 400 kDa, whereas HFB is heterogeneous and of low molecular mass. On Western blots, antibody to HFA detected both high-molecular-mass mucin and a 90 kDa protein in homogenates of LS174T cells. Antibody to HFB detected a major 70 kDa band as well as higher-molecular-mass species. In tissue sections of normal colon and colon cancers, antibody to HFA showed both cytoplasmic and extracellular staining, whereas antibody to HFB generally stained only cytoplasmic antigens. These results indicate that anti-HFB antibody is specific for apo-mucin, whereas anti-HFA antibody is specific for GalNAc-apo-mucin.
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PMID:Deglycosylation of mucin from LS174T colon cancer cells by hydrogen fluoride treatment. 277 37


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