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Journal articles on the topic 'Endoglycosidase'

Author: Grafiati

Published: 4 June 2021

Last updated: 28 January 2023

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1

Gallagher, J. T., A. Walker, M. Lyon, and W. H. Evans. "Heparan sulphate-degrading endoglycosidase in liver plasma membranes." Biochemical Journal 250, no. 3 (1988): 719–26. http://dx.doi.org/10.1042/bj2500719.

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An endoglycosidase is described in isolated liver plasma membranes that brings about a rapid and selective degradation of membrane-associated heparan sulphate, pre-labelled biosynthetically with Na2(35)SO4. The enzyme attacked mainly the polysaccharide chains of a hydrophobic membrane proteoglycan and it had little effect on a proteoglycan that could be displaced from the membranes with 1.0 M-NaCl. The highest activity was measured in the pH range 7.5-8.0, and the enzyme was almost completely inhibited below pH 5.5. Breakdown of susceptible polysaccharide chains was fast, being complete in 20-

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2

Majumder, S., K. Brown, F. H. Qiu, and P. Besmer. "c-kit protein, a transmembrane kinase: identification in tissues and characterization." Molecular and Cellular Biology 8, no. 11 (1988): 4896–903. http://dx.doi.org/10.1128/mcb.8.11.4896-4903.1988.

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The proto-oncogene c-kit encodes a transmembrane kinase which is related to the receptors for colony-stimulating factor type 1 and platelet-derived growth factor, as well as to the immunoglobulin superfamily. Antibodies specific for the kinase domain of the P80 gag-kit protein of the Hardy-Zuckerman 4 feline sarcoma virus were prepared. These kit-specific antibodies were used to identify and characterize the c-kit protein in cat brain tissue. The c-kit protein product displays an autophosphorylating activity in immune complex kinase assays, and, in turn, this activity was used to identify the

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3

Majumder, S., K. Brown, F. H. Qiu, and P. Besmer. "c-kit protein, a transmembrane kinase: identification in tissues and characterization." Molecular and Cellular Biology 8, no. 11 (1988): 4896–903. http://dx.doi.org/10.1128/mcb.8.11.4896.

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The proto-oncogene c-kit encodes a transmembrane kinase which is related to the receptors for colony-stimulating factor type 1 and platelet-derived growth factor, as well as to the immunoglobulin superfamily. Antibodies specific for the kinase domain of the P80 gag-kit protein of the Hardy-Zuckerman 4 feline sarcoma virus were prepared. These kit-specific antibodies were used to identify and characterize the c-kit protein in cat brain tissue. The c-kit protein product displays an autophosphorylating activity in immune complex kinase assays, and, in turn, this activity was used to identify the

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4

Swedlow, J. R., R. L. Matteri, and H. Papkoff. "Deglycosylation of Gonadotropins with an Endoglycosidase." Experimental Biology and Medicine 181, no. 3 (1986): 432–37. http://dx.doi.org/10.3181/00379727-181-42277.

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5

Paton, B. C., and A. Poulos. "Analysis of the multiple forms of Gaucher spleen sphingolipid activator protein 2." Biochemical Journal 254, no. 1 (1988): 77–84. http://dx.doi.org/10.1042/bj2540077.

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Gaucher spleen sphingolipid activator protein 2 was fractionated into concanavalin A binding- and non-binding fractions. These fractions each contained several bands on non-denaturing polyacrylamide gel electrophoresis (PAGE). The two fractions were further fractionated by electroblotting the proteins from preparative gels onto nitrocellulose, staining with Ponceau S to locate the bands of protein and then eluting the protein components from the nitrocellulose. A total of ten fractions, each containing only one or two major components, was collected. All of these subfractions activated beta-gl

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6

Lublin, D. M., J. Krsek-Staples, M. K. Pangburn, and J. P. Atkinson. "Biosynthesis and glycosylation of the human complement regulatory protein decay-accelerating factor." Journal of Immunology 137, no. 5 (1986): 1629–35. http://dx.doi.org/10.4049/jimmunol.137.5.1629.

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Abstract The biosynthesis and oligosaccharide structure of the human complement regulatory glycoprotein decay-accelerating factor (DAF) were studied in erythrocytes and cell lines. Initial information relative to carbohydrate moieties of DAF was obtained by enzymatic digestions. The 74,000 Mr erythrocyte DAF was lowered 3000 by endoglycosidase F, whereas endoglycosidase H had no effect, indicating one N-linked complex-type unit. Treatment with endo-alpha-N-acetylgalactosaminidase to remove O-linked oligosaccharides resulted in a 48,000 Mr molecule (67% of the Mr shift being due to sialic acid)

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7

Torok, Rebeka, Felicia Auer, Robert Farsang, Eszter Jona, Gabor Jarvas, and Andras Guttman. "The Effect of Sample Glucose Content on PNGase F-Mediated N-Glycan Release Analyzed by Capillary Electrophoresis." Molecules 27, no. 23 (2022): 8192. http://dx.doi.org/10.3390/molecules27238192.

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Protein therapeutics have recently gained high importance in general health care along with applied clinical research. Therefore, it is important to understand the structure–function relationship of these new generation drugs. Asparagine-bound carbohydrates represent an important critical quality attribute of therapeutic glycoproteins, reportedly impacting the efficacy, immunogenicity, clearance rate, stability, solubility, pharmacokinetics and mode of action of the product. In most instances, these linked N-glycans are analyzed in their unconjugated form after endoglycosidase-mediated release

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8

Sugano, Wataru, Ryukichi Ryo, Nobuo Yamaguchi, and Yoichi Shibata. "Endoglycosidase H digestion of Yukb(Pena) alloantigen." Thrombosis Research 67, no. 2 (1992): 167–77. http://dx.doi.org/10.1016/0049-3848(92)90136-x.

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9

Tarentino, A. L., G. Quinones, L. M. Changchien, and T. H. Plummer. "Multiple endoglycosidase F activities expressed by Flavobacterium meningosepticum endoglycosidases F2 and F3. Molecular cloning, primary sequence, and enzyme expression." Journal of Biological Chemistry 268, no. 13 (1993): 9702–8. http://dx.doi.org/10.1016/s0021-9258(18)98405-x.

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10

Du, Jonathan J., Erik H. Klontz, Marcelo E. Guerin, Beatriz Trastoy, and Eric J. Sundberg. "Structural insights into the mechanisms and specificities of IgG-active endoglycosidases." Glycobiology 30, no. 4 (2019): 268–79. http://dx.doi.org/10.1093/glycob/cwz042.

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Abstract The conserved N-glycan on Asn297 of immunoglobulin G (IgG) has significant impacts on antibody effector functions, and is a frequent target for antibody engineering. Chemoenzymatic synthesis has emerged as a strategy for producing antibodies with homogenous glycosylation and improved effector functions. Central to this strategy is the use of enzymes with activity on the Asn297 glycan. EndoS and EndoS2, produced by Streptococcus pyogenes, are endoglycosidases with remarkable specificity for Asn297 glycosylation, making them ideal tools for chemoenzymatic synthesis. Although both enzyme

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11

Agelidis, Alex, Rahul K. Suryawanshi, Chandrashekhar D. Patil, Anaamika Campeau, David J. Gonzalez, and Deepak Shukla. "Dissociation of DNA damage sensing by endoglycosidase HPSE." iScience 24, no. 3 (2021): 102242. http://dx.doi.org/10.1016/j.isci.2021.102242.

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12

Kwong, F. Y., S. A. Baldwin, P. R. Scudder, S. M. Jarvis, M. Y. Choy та J. D. Young. "Erythrocyte nucleoside and sugar transport Endo-β-galactosidase and endoglycosidase-F digestion of partially purified human and pig transporter proteins". Biochemical Journal 240, № 2 (1986): 349–56. http://dx.doi.org/10.1042/bj2400349.

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Nucleoside- and glucose-transport proteins isolated from human erythrocyte membranes were photoaffinity-labelled with [3H]nitrobenzylthioinosine and [3H]cytochalasin B, respectively, and subjected to endo-beta-galactosidase or endoglycosidase-F digestion. Without enzyme treatment the two radiolabelled transporters migrated on SDS/polyacrylamide gels with the same apparent Mr (average) of 55,000. Apparent Mr (average) values after endo-beta-galactosidase digestion were 47,000 and 48,000 for the nucleoside and glucose transporters respectively, and 44,000 and 45,000 respectively after endoglycos

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13

Leushner, James R. A. "Partial characterization of the heteropolysaccharide associated with the 7S domain of type IV collagen from placenta." Biochemistry and Cell Biology 65, no. 5 (1987): 501–6. http://dx.doi.org/10.1139/o87-064.

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A major heteropolysaccharide fraction was isolated from the 7S domain of human placental type IV collagen. Analyses revealed that it was an asparagine-linked oligosaccharide. Characterization using molecular sieve chromatography, exoglycosidase and endoglycosidase digestion, and chemical analysis suggested a bianternnary complex with the following structure:[Formula: see text]A microheterogeneity was noted with respect to the addition of the fucose and sialic acid residues. Analysis of component polypeptides of the 7S fraction following endoglycosidase treatment suggested that the most obvious

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14

Yamamoto, Kenji, Kenya Fujimori, Yoshitaka Shimada, et al. "Chemo-enzymatic Syntheses of Bioactive Glycoconjugates Using Microbial Endoglycosidase." Journal of Applied Glycoscience 48, no. 2 (2001): 195–203. http://dx.doi.org/10.5458/jag.48.195.

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15

Liotta, Louis J., Ronald C. Bernotas, David B. Wilson, and Bruce Ganem. "A new class of endoglycosidase inhibitors. Studies on endocellulases." Journal of the American Chemical Society 111, no. 2 (1989): 783–85. http://dx.doi.org/10.1021/ja00184a084.

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16

Yamamoto, Kenji. "Chemo-Enzymatic synthesis of bioactive glycopeptide using microbial endoglycosidase." Journal of Bioscience and Bioengineering 92, no. 6 (2001): 493–501. http://dx.doi.org/10.1016/s1389-1723(01)80307-8.

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17

Trastoy, Beatriz. "Crystal structure of EndoS, an immunomodulatory endoglycosidase specific for human IgG antibodies." Acta Crystallographica Section A Foundations and Advances 70, a1 (2014): C256. http://dx.doi.org/10.1107/s2053273314097435.

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In order to evade host immune mechanisms, many bacteria secrete immunomodulatory enzymes. Streptococcus pyogenes, one of the most common human pathogens, secretes a large endoglycosidase, EndoS, which removes carbohydrates in a highly specific manner from IgG antibodies. This modification renders antibodies incapable of eliciting host effector functions through either complement or Fc γ receptors, providing the bacteria with a survival advantage. On account of this antibody-specific modifying activity, EndoS is being developed as a promising injectable therapeutic for autoimmune diseases that

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18

Sjögren, Jonathan, Weston B. Struwe, Eoin F. J. Cosgrave та ін. "EndoS2 is a unique and conserved enzyme of serotype M49 group A Streptococcus that hydrolyses N-linked glycans on IgG and α1-acid glycoprotein". Biochemical Journal 455, № 1 (2013): 107–18. http://dx.doi.org/10.1042/bj20130126.

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In this study, the endoglycosidase EndoS2 was characterized. The enzyme was found to be unique and conserved in serotype M49 of group A Streptococcus and to specifically cleave N-linked glycans on IgG and AGP.

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19

Zhang, Wei, Hong Wang, Hailin Tang, and Pengyuan Yang. "Endoglycosidase-Mediated Incorporation of18O into Glycans for Relative Glycan Quantitation." Analytical Chemistry 83, no. 12 (2011): 4975–81. http://dx.doi.org/10.1021/ac200753e.

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20

Goodfellow, Jonathan J., Kavitha Baruah, Keisuke Yamamoto, et al. "An Endoglycosidase with Alternative Glycan Specificity Allows Broadened Glycoprotein Remodelling." Journal of the American Chemical Society 134, no. 19 (2012): 8030–33. http://dx.doi.org/10.1021/ja301334b.

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21

Yamamoto, Kenji, Kenya Fujimori, Katsuji Haneda, Mamoru Mizuno, Toshiyuki Inazu, and Hidehiko Kumagai. "Chemoenzymatic synthesis of a novel glycopeptide using a microbial endoglycosidase." Carbohydrate Research 305, no. 3-4 (1997): 415–22. http://dx.doi.org/10.1016/s0008-6215(97)10018-0.

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22

Yamamoto, Kenji. "ChemInform Abstract: Chemoenzymatic Synthesis of Bioactive Glycopeptide Using Microbial Endoglycosidase." ChemInform 33, no. 31 (2010): no. http://dx.doi.org/10.1002/chin.200231283.

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23

Wang, Lai-Xi. "Chemoenzymatic synthesis of glycopeptides and glycoproteins through endoglycosidase-catalyzed transglycosylation." Carbohydrate Research 343, no. 10-11 (2008): 1509–22. http://dx.doi.org/10.1016/j.carres.2008.03.025.

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24

Boué, D. R., and T. W. Lebien. "Structural characterization of the human B lymphocyte-restricted differentiation antigen CD22. Comparison with CD21 (complement receptor type 2/Epstein-Barr virus receptor)." Journal of Immunology 140, no. 1 (1988): 192–99. http://dx.doi.org/10.4049/jimmunol.140.1.192.

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Abstract CD22 and CD21 are glycoproteins primarily expressed on normal and neoplastic human B cells. The surface expression of these two molecules parallel each other during normal B cell differentiation, and the reported relative mobilities for CD22 and CD21 are 130/140 kDa and 140 kDa, respectively. Herein we present a detailed analysis of the biosynthesis and structure of CD22 and also compare it directly to CD21. Electrophoresis under reducing and nonreducing conditions suggested that CD22 and CD21 may have similarities in intra-chain disulfide bond formation. Biosynthesis and processing o

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25

Chawla, D., and R. C. Hughes. "Effects of brefeldin A on oligosaccharide processing. Evidence for decreased branching of complex-type glycans and increased formation of hybrid-type glycans." Biochemical Journal 279, no. 1 (1991): 159–65. http://dx.doi.org/10.1042/bj2790159.

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Brefeldin A (BFA), a drug that induces redistribution of Golgi-apparatus proteins into the endoplasmic reticulum, was used to determine the role of subcellular compartmentalization in the processing of asparagine-linked oligosaccharides. Baby-hamster kidney cells were pulse-labelled with [3H]mannose for 30-60 min and chased for up to several hours in the presence or in the absence of BFA or labelled continuously for several hours with and without the drug. Cellular glycoproteins were digested to glycopeptides with Pronase and either fractionated into glycan classes by lectin affinity chromatog

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26

Verheijden, G. F., W. H. Moolenaar, and H. L. Ploegh. "Retention of epidermal growth factor receptors in the endoplasmic reticulum of adenovirus-infected cells." Biochemical Journal 282, no. 1 (1992): 115–21. http://dx.doi.org/10.1042/bj2820115.

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The epidermal growth factor (EGF) receptor is down-regulated during early infection with adenovirus, and this has been attributed to accelerated internalization and degradation of the receptor in the absence of ligand (Carlin, Tollefson, Brady, Hoffman & Wold (1989) Cell 57, 135-144]. Using pulse-chase analysis, we show that loss of functional EGF receptors after infection of human KB and A431 cells with adenovirus type 5 is accompanied by accumulation of a receptor precursor that remains fully sensitive to endoglycosidase H, indicative of retention in the endoplasmic reticulum. A truncate

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27

Davidson, S. K., and L. A. Hunt. "Hazelhurst-vesicular-stomatitis-virus G and Sindbis-virus E1 glycoproteins undergo similar host-cell-dependent variation in oligosaccharide processing." Biochemical Journal 229, no. 1 (1985): 47–55. http://dx.doi.org/10.1042/bj2290047.

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We have examined and compared the host-cell-dependent glycosylation of the G glycoprotein of vesicular-stomatitis virus (Hazelhurst strain) and the E1 and E2 glycoproteins of Sindbis virus replicated by baby-hamster kidney, chicken-embryo fibroblast and mouse L929 monolayer cell cultures. The results of endo-beta-N-acetylglucosaminidase H digestion of viral proteins labelled with [3H]mannose or leucine and Pronase-digested glycopeptides labelled with [3H]mannose indicated that both the G protein and the E1 protein contained a similar mixture of endoglycosidase-resistant oligosaccharides of the

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28

Prandini, M. H., A. Reboul, and M. G. Colomb. "Biosynthesis of complement C1 inhibitor by Hep G2 cells. Reactivity of different glycosylated forms of the inhibitor with C1s." Biochemical Journal 237, no. 1 (1986): 93–98. http://dx.doi.org/10.1042/bj2370093.

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The biosynthesis of C1 Inh (C1 inhibitor) was studied in a human hepatoma cell line (Hep G2) by metabolic labelling, immunoprecipitation with anti-(C1 Inh) serum, analysis on SDS/polyacrylamide gel slabs and fluorography. Two forms of C1 Inh are secreted by Hep G2: a minor form of Mr 90,000 and a major form of Mr approximately 100,000. The latter form is also found in small amounts intracellularly in co-existence with an 80,000-Mr form. Accumulation of the 80,000-Mr C1 Inh is favoured when the cells are labelled at 23 degrees C instead of 37 degrees C or when they are treated with monensin. In

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29

Terman, B. I., J. F. Reece, R. D. Brown та P. A. Insel. "The oligosaccharide component of α 1-adrenergic receptors from BC3H1 and DDT1 muscle cells. Studies with glycosidases and photoaffinity labelling of intact cells". Biochemical Journal 253, № 2 (1988): 363–70. http://dx.doi.org/10.1042/bj2530363.

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In this study, we clarify the structural aspects of the oligosaccharides associated with the alpha 1-adrenergic receptor in two muscle cell lines. Photoaffinity labelling of intact BC3H1 or DDT1 muscle cells with 2-[4-(4-azido-3-[125I]iodobenzoyl)piperazin-1-yl]-4-amino-6, 7-dimethoxyquinazoline ([125I]azidoprazosin) followed by SDS/polyacrylamide-gel electrophoresis (PAGE) and autoradiography revealed specifically labelled proteins of molecular mass = 87,000 and 81,000, respectively. Treatment of photoaffinity-labelled receptors in DDT1 cells with 33 u. of endoglycosidase F/ml for 24 h result

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30

Sztul, E. S., K. E. Howell, and G. E. Palade. "Biogenesis of the polymeric IgA receptor in rat hepatocytes. I. Kinetic studies of its intracellular forms." Journal of Cell Biology 100, no. 4 (1985): 1248–54. http://dx.doi.org/10.1083/jcb.100.4.1248.

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The polymeric IgA receptor (or secretory component [SC]) is a major biliary secretory protein in the rat. It was identified as an 80,000-mol-wt (80 K) glycoprotein by coprecipitation (with IgA) by anti-IgA antibodies (Sztul, E. S., K. E. Howell, and G. E. Palade, 1983, J. Cell Biol., 97:1582-1591) and was used as antigen to raise anti-SC antibodies in rabbits. Pulse labeling with [35S]cysteine in vivo, followed by the immunoprecipitation of solubilized total microsomal fractions with anti-SC sera, made possible the identification of three intracellular forms of SC (all apparently membrane prot

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31

Aytenfisu, Asaminew H., Daniel Deredge, Erik H. Klontz, Jonathan Du, Eric J. Sundberg, and Alexander D. MacKerell. "Insights into substrate recognition and specificity for IgG by Endoglycosidase S2." PLOS Computational Biology 17, no. 7 (2021): e1009103. http://dx.doi.org/10.1371/journal.pcbi.1009103.

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Antibodies bind foreign antigens with high affinity and specificity leading to their neutralization and/or clearance by the immune system. The conserved N-glycan on IgG has significant impact on antibody effector function, with the endoglycosidases of Streptococcus pyogenes deglycosylating the IgG to evade the immune system, a process catalyzed by the endoglycosidase EndoS2. Studies have shown that two of the four domains of EndoS2, the carbohydrate binding module (CBM) and the glycoside hydrolase (GH) domain are critical for catalytic activity. To yield structural insights into contributions

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32

Hulett, Mark D., June R. Hornby, Stephen J. Ohms, et al. "Identification of Active-Site Residues of the Pro-Metastatic Endoglycosidase Heparanase†." Biochemistry 39, no. 51 (2000): 15659–67. http://dx.doi.org/10.1021/bi002080p.

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33

Nandakumar, Kutty Selva, Mattias Collin, Arne Olsén, et al. "Endoglycosidase treatment abrogates IgG arthritogenicity: Importance of IgG glycosylation in arthritis." European Journal of Immunology 37, no. 10 (2007): 2973–82. http://dx.doi.org/10.1002/eji.200737581.

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34

Yu, Zixiang, Xinyuan Zhao, Fang Tian, et al. "Sequential fragment ion filtering and endoglycosidase-assisted identification of intact glycopeptides." Analytical and Bioanalytical Chemistry 409, no. 12 (2017): 3077–87. http://dx.doi.org/10.1007/s00216-017-0195-z.

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35

Hazen, Kevin C., and Pati M. Glee. "Hydrophobic cell wall protein glycosylation by the pathogenic fungus Candida albicans." Canadian Journal of Microbiology 40, no. 4 (1994): 266–72. http://dx.doi.org/10.1139/m94-043.

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Cell surface hydrophobicity influences adhesion and virulence of the opportunistic fungal pathogen Candida albicans. Previous studies have shown that cell surface hydrophobicity is due to specific proteins that are exposed on hydrophobic cells but are masked by long fibrils on hydrophilic cells. This observation suggests that hydrophobic cell wall proteins may contain little or no mannosylation. In the present study, the glycosylation levels of three hydrophobic cell wall proteins (molecular mass range between 36 and 40 kDa) derived from yeast cells were examined. One hydrophilic protein (90 k

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36

Kim, L. T., S. Ishihara, C. C. Lee, S. K. Akiyama, K. M. Yamada, and F. Grinnell. "Altered glycosylation and cell surface expression of beta 1 integrin receptors during keratinocyte activation." Journal of Cell Science 103, no. 3 (1992): 743–53. http://dx.doi.org/10.1242/jcs.103.3.743.

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We studied the mechanism by which cell adhesiveness becomes activated when keratinocytes are removed from skin and placed into cell culture. Our results suggest that activation involves altered beta 1 integrin subunit glycosylation accompanied by an increase in cell surface beta 1 integrin receptors. Activated keratinocytes contained two forms of the beta 1 integrin subunit, approximately 93 kDa and approximately 113 kDa. As shown by pulse-chase experiments, the smaller represented the cytoplasmic precursor of the larger, and only the 113 kDa mature form was detected in integrin receptors expr

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37

Schweitzer, P. A., S. E. Taylor, and L. D. Shultz. "Synthesis of abnormal immunoglobulins by hybridomas from autoimmune "viable motheaten" mutant mice." Journal of Cell Biology 114, no. 1 (1991): 35–43. http://dx.doi.org/10.1083/jcb.114.1.35.

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Secretory defects in abnormal plasma cells, called Mott cells, that appear in lymphoid tissues of spontaneously autoimmune, "viable motheaten" (mev/mev) mice lead to deposition of immunoglobulin in RER-bound vesicles. Such vesicles have been termed Russel bodies. Cells with Russel bodies can also be observed rarely in normal animals, usually as a result of extreme antigenic loads or pathologic states. To understand why these abnormal cells appear commonly in mev/mev mice, we have established a panel of hybridomas that contain Russell bodies. Using immunochemical analysis and immunoelectron mic

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38

Kleinberg, M. E., D. Rotrosen, and H. L. Malech. "Asparagine-linked glycosylation of cytochrome b558 large subunit varies in different human phagocytic cells." Journal of Immunology 143, no. 12 (1989): 4152–57. http://dx.doi.org/10.4049/jimmunol.143.12.4152.

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Abstract Cytochrome b558, an essential component of the respiratory burst of phagocytic cells, is the terminal electron donor to molecular oxygen that results in the formation of superoxide anion (O2-.). It is an integral membrane heterodimer that in neutrophils consists of a 22-kDa small subunit and a highly glycosylated 91-kDa large subunit. Identical core proteins often differ in glycosylation in different cell types and with some membrane glycoproteins, the glycosylation state may markedly affect function. In the present study, antisera reactive with cytochrome b558 large subunit was used

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39

Haworth, R. S., O. Fröhlich, and L. Fliegel. "Multiple carbohydrate moieties on the Na+/H+ exchanger." Biochemical Journal 289, no. 3 (1993): 637–40. http://dx.doi.org/10.1042/bj2890637.

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Affinity-purified antibodies against the C-terminal region of the Na+/H+ exchanger (NHE-1) were used to analyse the carbohydrate moiety of the protein. The Na+/H+ exchanger in human placental brush-border membranes has an apparent molecular mass of 105 kDa. Incubation of intact or detergent-solubilized membranes with glycopeptidase F removed the carbohydrate moiety and increased the apparent mobility of the exchanger. Digestion with endoglycosidase-F caused a similar change in mobility, but endoglycosidase-H had no effect, suggesting that the placental Na+/H+ exchanger is a glycoprotein of the

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40

Hancock, Larry W., та Glyn Dawson. "Evidence for two catabolic endoglycosidase activities in β-mannosidase-deficient goat fibroblasts". Biochimica et Biophysica Acta (BBA) - Molecular Cell Research 928, № 1 (1987): 13–21. http://dx.doi.org/10.1016/0167-4889(87)90080-2.

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41

Nakajima, Motowo, Tatsuro Irimura, and Garth L. Nicolson. "Tumor metastasis-associated heparanase (heparan sulfate endoglycosidase) activity in human melanoma cells." Cancer Letters 31, no. 3 (1986): 277–83. http://dx.doi.org/10.1016/0304-3835(86)90148-5.

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42

Duvet, Sandrine, Dounia Mouajjah, Romain Péanne, et al. "Use of Endoglycosidase H as a diagnostic tool for MAN1B1‐CDG patients." ELECTROPHORESIS 39, no. 24 (2018): 3133–41. http://dx.doi.org/10.1002/elps.201800020.

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43

YAMAMOTO, K., K. FUJIMORI, K. HANEDA, M. MIZUNO, T. INAZU, and H. KUMAGAI. "ChemInform Abstract: Chemoenzymatic Synthesis of a Novel Glycopeptide Using a Microbial Endoglycosidase." ChemInform 29, no. 35 (2010): no. http://dx.doi.org/10.1002/chin.199835257.

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44

Carlsson, S. R. "Changes in glycan branching and sialylation of the Thy-1 antigen during normal differentiation of mouse T-lymphocytes." Biochemical Journal 226, no. 2 (1985): 519–25. http://dx.doi.org/10.1042/bj2260519.

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The glycans of the Thy-1 antigen present on thymocytes and lymph-node T-lymphocytes were investigated after external labelling of the cells. Neuraminidase, endoglycosidase H and endoglycosidase F were used in combination with sodium dodecyl sulphate/polyacrylamide-gel electrophoresis and isoelectric focusing in order to characterize the nature of the glycans on 125I-labelled and immunoprecipitated Thy-1. Glycopeptides were prepared from Thy-1 obtained from cells labelled by periodate/boro[3H]hydride treatment. The glycopeptides were separated by affinity chromatography on concanavalin A-Sephar

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Hunt, L. A., and S. E. Wright. "Both acidic-type and neutral-type asparaginyl-oligosaccharides of host-cell glycoproteins are altered in Rous-sarcoma-virus-transformed chick-embryo fibroblasts." Biochemical Journal 229, no. 2 (1985): 441–51. http://dx.doi.org/10.1042/bj2290441.

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In comparisons of [3H]mannose-labelled glycopeptides from chick-embryo fibroblasts infected and transformed with non-defective Prague C Rous-sarcoma virus and from untransformed fibroblasts infected with a transformation-defective derivative of Prague C Rous-sarcoma virus, we have detected transformation-dependent alterations in both the acidic-type and the neutral-type asparagine-linked oligosaccharides of cellular glycoproteins. Pronase-digested glycopeptides were analysed by the combined techniques of gel filtration, exo- and endo-glycosidase digestion and concanavalin A-agarose affinity ch

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Hernández, Mariana V., Diana P. Wehrendt, and Carlos O. Arregui. "The Protein Tyrosine Phosphatase PTP1B Is Required for Efficient Delivery of N-Cadherin to the Cell Surface." Molecular Biology of the Cell 21, no. 8 (2010): 1387–97. http://dx.doi.org/10.1091/mbc.e09-10-0880.

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PTP1B bound to mature N-cadherin promotes the association of β-catenin into the complex, the stable expression of the complex at cell surface, and cadherin-mediated adhesion. Here we show that PTP1B is also required for N-cadherin precursor trafficking through early stages of the secretory pathway. This function does not require association of PTP1B with the precursor. In PTP1B null cells, the N-cadherin precursor showed higher sensitivity to endoglycosidase H than in cells reconstituted with the wild-type enzyme. It also showed slower kinetics of ER-to-Golgi translocation and processing. Traf

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Ohara, J., J. E. Coligan, K. Zoon, W. L. Maloy, and W. E. Paul. "High-efficiency purification and chemical characterization of B cell stimulatory factor-1/interleukin 4." Journal of Immunology 139, no. 4 (1987): 1127–34. http://dx.doi.org/10.4049/jimmunol.139.4.1127.

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Abstract B cell stimulatory factor-1/interleukin 4, a lymphokine produced by phorbol ester activated-EL-4 thymoma cells, was purified to homogeneity in good yield by a two-step purification procedure, using affinity chromatography and a single subsequent round of reverse-phase high-performance liquid chromatography. The N-terminal sequence of the first 24 amino acids was consistent with that inferred from the nucleotide sequence of BSF-1 cDNA clones. Amino acid composition analysis also agreed well with that predicted from the nucleotide sequence. A rabbit antibody to a peptide corresponding t

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GROTJAN, H. EDWARD, and LAURENCE A. COLE. "Ovine and Human Luteinizing Hormone Enzymatically Deglycosylated with Endoglycosidase F Are Biologically Active." Annals of the New York Academy of Sciences 513, no. 1 Cell Biology (1987): 329–31. http://dx.doi.org/10.1111/j.1749-6632.1987.tb25031.x.

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Levy-Adam, Flonia, Ghada Abboud-Jarrous, Marco Guerrini, Daniela Beccati, Israel Vlodavsky, and Neta Ilan. "Identification and Characterization of Heparin/Heparan Sulfate Binding Domains of the Endoglycosidase Heparanase." Journal of Biological Chemistry 280, no. 21 (2005): 20457–66. http://dx.doi.org/10.1074/jbc.m414546200.

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Barbirz, Stefanie, Jürgen J. Müller, Charlotte Uetrecht, Alvin J. Clark, Udo Heinemann, and Robert Seckler. "Crystal structure ofEscherichia coliphage HK620 tailspike: podoviral tailspike endoglycosidase modules are evolutionarily related." Molecular Microbiology 69, no. 2 (2008): 303–16. http://dx.doi.org/10.1111/j.1365-2958.2008.06311.x.

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