Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: EC:3.5.1.52 (PNGase F)
1,527 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The rat major histocompatibility complex class I antigens RT1.Au and RT1.Eu from the u haplotype and RT1. An from the n haplotype were labeled with 14C-asparagine or with 3H-fucose, mannose, galactose, and N-acetylglucosamine. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis analysis showed complete removal of radioactivity from the sugar-labeled antigen heavy chains by digestion with glycopeptidase F, an enzyme that removes N-linked glycans completely. High performance liquid chromatography analysis of the tryptic digests of the mixed sugar-labeled and asparagine-labeled antigens demonstrated that all the sugar-labeled peptides were coincident with asparagine-labeled peptides. The An antigen showed three glycopeptides, each of which had different amounts of sugar radioactivity. The antigens Au and Eu showed two glycopeptides with different amounts of radioactivity but at identical positions in the two antigens. Antigen Eu had an additional glycopeptide with a lower amount of radioactivity. The positions of the glycopeptides from the Au and Eu antigens were different from those of the An antigen. The peptide profiles of the 14C-asparagine-labeled Au and Eu antigens demonstrated distinct differences between the molecules. The results of this study show that: (a) all the glycans on rat class I antigens are N-linked, as they are on H-2 and HLA class I antigens; (b) there are compositional differences among the glycans in each of the three antigens; (c) the glycosylation pattern of the rat class I antigens is similar to that of the mouse class I antigens, which contain two or three glycans, in contrast to that of the human class I antigens, which contain only one glycan; and (d) the antigens Au and Eu from the same haplotype are more closely related to each other than they are to the An antigen.
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PMID:Carbohydrate moieties of rat MHC class I antigens. 365 37

N-glycanase, an endoglycosidase that cleaves the bond between asparagine and glucosamine, releases oligosaccharides with various degree of sulfation from endothelial cell fibronectin. As shown by analysis by polyacrylamide gel electrophoresis of culture medium conditioned by cells exposed to [35S]sulfate, endothelial cell fibronectin is one of a number of glycoproteins bearing sulfated oligosaccharides, synthesized by this cell type.
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PMID:N-glycansulfated fibronectin: one of the several sulfated glycoproteins synthesized by endothelial cells in culture. 366 21

Lectins were isolated from fruits and leaves of Clerodendron trichotomum by affinity chromatography on lactamyl-Sepharose. The purified lectins (C. trichotomum agglutinin: CTA) were homogeneous on SDS/polyacrylamide gel electrophoresis, and the carbohydrate moiety was characterized by physicochemical and immunochemical methods. The asparagine-linked oligosaccharides were released by treatment with N-oligosaccharide glycopeptidase (almond, EC 3.5.1.52) of peptic glycopeptides obtained from fruit CTA, and separated by gel filtration and thin-layer chromatography. The structure of the predominant oligosaccharide was determined as Xyl beta 1----2 (Man alpha 1----6)(Man alpha 1----3)Man beta 1----4GlcNAc beta 1----4(Fuc alpha 1----3)GlcNAc by high-performance liquid chromatography, sugar analysis and 1H-NMR spectroscopy. The reactivity of the carbohydrate moiety of CTA toward various lectins was studied. Fruit and leaf CTAs were applied to polyacrylamide gel electrophoresis, transferred to nitrocellulose sheets and detected with horseradish-peroxidase-conjugated lectins. Concanavalin A, lentil lectin, pea lectin, Vicia faba lectin and Ulex europeus agglutinin I, but not wheat germ lectin, bound to fruit CTA. The results indicate new binding properties of these plant lectins: a beta-xylosyl residue substituted at C-2 of the beta-mannosyl residue of N-linked oligosaccharide does not affect the binding with mannose-specific lectins, lentil, pea and Vicia faba lectins can bind to N-linked oligosaccharides containing an alpha-L-fucosyl residue attached to C-3 of the asparagine-linked N-acetyl-D-glucosamine residue, and Ulex europeus agglutinin I can bind to the (alpha 1----3)-linked fucose residue of the N-linked oligosaccharide.
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PMID:Characterization of the carbohydrate moiety of Clerodendron trichotomum lectins. Its structure and reactivity toward plant lectins. 379 15

Asparagine-linked oligosaccharides were released quantitatively by N-oligosaccharide glycopeptidase (almond) digestion from human thyroglobulins prepared from thyroid glands of normal subjects and patients with several pathological conditions. The pyridylamino derivatives of the oligosaccharides were prepared and analyzed by high-performance liquid chromatography. The content of high-mannose-type oligosaccharides was comparable to that of the complex type in normal thyroglobulins. Man9GlcNAc2 was the predominant component in the high-mannose-type region, while biantennary oligosaccharides with fucose were the major components in the complex-type region. High-mannose-type oligosaccharides were markedly decreased in thyroglobulins prepared from patients with various disorders, such as Basedow's disease, papillary carcinoma, and adenomatous goiter, whereas they were appreciably increased in thyroglobulin from diffuse goiter.
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PMID:Comparative study of the oligosaccharides of human thyroglobulins obtained from normal subjects and patients with various diseases. 384 Apr 70

In a series of mammalian and avian tissues, asparagine-linked oligosaccharides of glycoproteins have been localized histochemically by means of combined periodic acid-Schiff (PAS) and almond glycopeptidase digestion procedures. According to the present results, the particular saccharide residues were found to be localized primarily in glycoproteins of connective and muscular tissue elements but were hardly visualizable or absent in glycoproteins of epithelial tissue elements. In view of the substrate specificity of almond glycopeptidase and the known staining selectivity of the PAS reaction, the majority of connective and muscular tissue elements are thought to be the main sites where plasma types of glycoproteins are involved.
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PMID:The histochemistry of asparagine-linked oligosaccharides of glycoproteins in mammalian and avian tissues as studied by digestion with almond glycopeptidase. 392 25

A glycoprotein that circulates in human blood, binds to the surface of platelets and white cells and also binds serotonin with high affinity and specificity has previously been purified and partially characterized. This glycoprotein has been called serotonectin. Antibodies raised against serotonectin inhibited the uptake of [3H]serotonin by platelets. We now report on the amino acid and carbohydrate composition of this protein as well as on some of the properties of the protein from which the carbohydrate moiety was removed. Serotonectin (apparent molecular weight 200 000; as judged by SDS-polyacrylamide gel electrophoresis) is an acidic protein that contains about 13% carbohydrate (w/w) consisting of mannose, galactose, glucosamine and sialic acid in a molar ratio of 2:1:4:0.8. Initial characterization suggests that serotonectin is a sialoglycoprotein of complex-type oligosaccharide N-linked to asparagine through N-acetylglucosamine. Treatment of serotonectin with neuraminidase resulted in a quantitative release of sialic acid without loss of antigenicity or binding capacity for [3H]serotonin. Treatment of desialylated serotonectin under non-denaturing conditions with almond glycopeptidase A resulted in 60-80% release of sugar. The protein moiety of the glycopeptidase-digested material showed no change in the capacity to bind [3H]serotonin and exhibited the same antigenic properties as untreated serotonectin. These data show the non-involvement of the carbohydrate moiety of human serotonectin in the mechanism of binding serotonin but the possible contribution of this moiety to a tighter interaction with the serotonectin receptor.
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PMID:Human serotonectin: a blood glycoprotein that binds serotonin. Chemical and physiological characterization. 394 85

Endo-beta-N-acetylglucosaminidase F (Endo F) and peptide:N-glycosidase F (PNGase F) were purified from cultures of Flavobacterium meningosepticum by ammonium sulfate precipitation followed by gel filtration on TSK HW-55(S). This system separated the two enzymes and provided PNGase F in a high state of purity, but the basis for the resolution appeared to be hydrophobic interaction and not molecular size. Studies using purified Endo F and PNGase F with defined glycopeptides demonstrated that Endo F was somewhat similar to Endo H in that it hydrolyzed many, but not all, high-mannose and hybrid oligosaccharides, as well as complex biantennary oligosaccharides. PNGase F, in contrast, hydrolyzed all classes of asparagine-linked glycans examined, provided both the alpha-amino and carboxyl groups of the asparagine residue were in peptide linkage. Deglycosylation studies with PNGase F revealed that many proteins in their native conformation were susceptible to this enzyme but that prior denaturation in sodium dodecyl sulfate greatly decreased the amount of enzyme required for complete carbohydrate removal.
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PMID:Deglycosylation of asparagine-linked glycans by peptide:N-glycosidase F. 406 49

Taka-amylase A (1,4-alpha-D-glucan glucanohydrolase, EC 3.2.1.1), which contains a single asparagine-linked oligosaccharide unit, was digested with almond glycopeptidase immobilized on Sepharose 6B at 20 degrees C for 4 h. A maximum of 10% of the parent protein was isolated as apoprotein by column chromatography on Con-A Sepharose. The characteristics of the apoprotein were compared to those of the native Taka-amylase A. The removal of the sugar chain from Taka-amylase. A caused no change in the pH-activity profile or in kinetic parameters of the hydrolysis of soluble starch. The stability of the apoprotein toward changing pH and digestion by proteases did not show any appreciable difference from that of the native Taka-amylase. These results suggest that the carbohydrate moiety of Taka-amylase A is not an essential participant in the catalysis.
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PMID:Isolation and characterization of Taka-amylase A apoprotein deglycosylated by digestion with almond glycopeptidase immobilized on Sepharose. 618 19

To determine the histochemical localization of asparagine-linked oligosaccharides of glycoproteins in a series of different mammalian and avian tissues, the effects of digestion with N-oligosaccharide glycopeptidase upon certain lectin-peroxidase-diaminobenzidine reactions of the histological structures involved have been studied by light microscopy. Throughout the tissues examined, asparagine-linked oligosaccharides of glycoproteins were localized mainly in histological structures of connective and muscular tissues, but were hardly or not visualized in those of epithelial tissues. These results appear to lead to the concept that connective and muscular tissues represent the main sites where plasma types of glycoproteins are involved in mammalian and avian species.
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PMID:Effects of digestion with N-oligosaccharide glycopeptidase upon certain lectin-peroxidase-diaminobenzidine reactions of glycoproteins in mammalian and avian tissues. 633 76

Isolated plasma membranes from rat liver and ascites hepatoma cells were shown by SDS-polyacrylamide gel electrophoresis and concanavalin A reactivity to contain a variety of glycoproteins having asparagine-linked oligosaccharides. Membrane oligosaccharides were released by almond glycopeptidase digestion, and the pyridylamino derivatives were analyzed by high-performance liquid chromatography. Forty-four percent of the total carbohydrates in the original membranes were released and suggested to be of the complex type. Hepatoma membranes showed different oligosaccharide patterns from normal.
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PMID:Analysis of asparagine-linked oligosaccharides from plasma membranes of rat normal liver and ascites hepatoma cells. 647 25


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