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Journal articles on the topic 'Glycosylation method'

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Published: 4 June 2021

Last updated: 7 February 2022

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1

Noyori, Ryoji, and Isao Kurimoto. "Electrochemical glycosylation method." Journal of Organic Chemistry 51, no. 22 (1986): 4320–22. http://dx.doi.org/10.1021/jo00372a050.

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2

Pal, Rita, Anupama Das, and Narayanaswamy Jayaraman. "One-pot oligosaccharide synthesis: latent-active method of glycosylations and radical halogenation activation of allyl glycosides." Pure and Applied Chemistry 91, no. 9 (2019): 1451–70. http://dx.doi.org/10.1515/pac-2019-0306.

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Abstract Chemical glycosylations occupy a central importance to synthesize tailor-made oligo- and polysaccharides of functional importance. Generation of the oxocarbenium ion or the glycosyl cation is the method of choice in order to form the glycosidic bond interconnecting a glycosyl moiety with a glycosyl/aglycosyl moiety. A number of elegant methods have been devised that allow the glycosyl cation formation in a fairly stream-lined manner to a large extent. The latent-active method provides a powerful approach in the protecting group controlled glycosylations. In this context, allyl glycosi

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3

Hsu, Mei-Yuan, Sarah Lam, Chia-Hui Wu, Mei-Huei Lin, Su-Ching Lin, and Cheng-Chung Wang. "Direct Dehydrative Glycosylation Catalyzed by Diphenylammonium Triflate." Molecules 25, no. 5 (2020): 1103. http://dx.doi.org/10.3390/molecules25051103.

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Methods for direct dehydrative glycosylations of carbohydrate hemiacetals catalyzed by diphenylammonium triflate under microwave irradiation are described. Both armed and disarmed glycosyl-C1-hemiacetal donors were efficiently glycosylated in moderate to excellent yields without the need for any drying agents and stoichiometric additives. This method has been successfully applied to a solid-phase glycosylation.

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4

Pugalenthi, Ganesan, Varadharaju Nithya, Kuo-Chen Chou, and Govindaraju Archunan. "Nglyc: A Random Forest Method for Prediction of N-Glycosylation Sites in Eukaryotic Protein Sequence." Protein & Peptide Letters 27, no. 3 (2020): 178–86. http://dx.doi.org/10.2174/0929866526666191002111404.

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Background: N-Glycosylation is one of the most important post-translational mechanisms in eukaryotes. N-glycosylation predominantly occurs in N-X-[S/T] sequon where X is any amino acid other than proline. However, not all N-X-[S/T] sequons in proteins are glycosylated. Therefore, accurate prediction of N-glycosylation sites is essential to understand Nglycosylation mechanism. Objective: In this article, our motivation is to develop a computational method to predict Nglycosylation sites in eukaryotic protein sequences. Methods: In this article, we report a random forest method, Nglyc, to predic

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5

Yang, Weizhun, Bo Yang, Sherif Ramadan, and Xuefei Huang. "Preactivation-based chemoselective glycosylations: A powerful strategy for oligosaccharide assembly." Beilstein Journal of Organic Chemistry 13 (October 9, 2017): 2094–114. http://dx.doi.org/10.3762/bjoc.13.207.

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Most glycosylation reactions are performed by mixing the glycosyl donor and acceptor together followed by the addition of a promoter. While many oligosaccharides have been synthesized successfully using this premixed strategy, extensive protective group manipulation and aglycon adjustment often need to be performed on oligosaccharide intermediates, which lower the overall synthetic efficiency. Preactivation-based glycosylation refers to strategies where the glycosyl donor is activated by a promoter in the absence of an acceptor. The subsequent acceptor addition then leads to the formation of t

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6

Polonik, S. G. "Glycosylation of Shikonin by the Helferich method." Chemistry of Natural Compounds 45, no. 2 (2009): 247–48. http://dx.doi.org/10.1007/s10600-009-9286-1.

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7

Mastihubová, Mária, and Monika Poláková. "A selective and mild glycosylation method of natural phenolic alcohols." Beilstein Journal of Organic Chemistry 12 (March 15, 2016): 524–30. http://dx.doi.org/10.3762/bjoc.12.51.

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Several bioactive natural p-hydroxyphenylalkyl β-D-glucopyranosides, such as vanillyl β-D-glucopyranoside, salidroside and isoconiferin, and their glycosyl analogues were prepared by a simple reaction sequence. The highly efficient synthetic approach was achieved by utilizing acetylated glycosyl bromides as well as aromatic moieties and mild glycosylation promoters. The aglycones, p-O-acetylated arylalkyl alcohols, were prepared by the reduction of the corresponding acetylated aldehydes or acids. Various stereoselective 1,2-trans-O-glycosylation methods were studied, including the DDQ–iodine o

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8

Kochetkov, Nicolay K., Evgeny M. Klimov, Nelly N. Malysheva, and Alexey V. Demchenko. "Stereospecific 1,2-cis-glycosylation: a modified thiocyanate method." Carbohydrate Research 232, no. 1 (1992): C1—C5. http://dx.doi.org/10.1016/s0008-6215(00)91007-3.

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9

Al-Maharik, Nawaf, and Nigel P. Botting. "An Efficient Method for the Glycosylation of Isoflavones." European Journal of Organic Chemistry 2008, no. 33 (2008): 5622–29. http://dx.doi.org/10.1002/ejoc.200800803.

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10

Matwiejuk, Martin, and Joachim Thiem. "New Method for Regioselective Glycosylation Employing Saccharide Oxyanions." European Journal of Organic Chemistry 2011, no. 29 (2011): 5860–78. http://dx.doi.org/10.1002/ejoc.201100861.

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11

Han, Mark S., and John T. Simpson. "A Method for Mapping Glycosylation Sites in Proteins." Journal of Biomolecular Techniques : JBT 28, no. 4 (2017): 142–49. http://dx.doi.org/10.7171/jbt.17-2804-001.

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12

Kochetkov, Nicolay K., Evgeny M. Klimov, Nelly N. Malysheva, and Alexey V. Demchenko. "A new stereospecific method for 1,2-cis-glycosylation." Carbohydrate Research 212 (June 1991): 77–91. http://dx.doi.org/10.1016/0008-6215(91)84047-i.

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13

Chang, Deborah, William E. Hackett, Lei Zhong, Xiu-Feng Wan, and Joseph Zaia. "Measuring Site-specific Glycosylation Similarity between Influenza a Virus Variants with Statistical Certainty." Molecular & Cellular Proteomics 19, no. 9 (2020): 1533–45. http://dx.doi.org/10.1074/mcp.ra120.002031.

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Influenza A virus (IAV) mutates rapidly, resulting in antigenic drift and poor year-to-year vaccine effectiveness. One challenge in designing effective vaccines is that genetic mutations frequently cause amino acid variations in IAV envelope protein hemagglutinin (HA) that create new N-glycosylation sequons; resulting N-glycans cause antigenic shielding, allowing viral escape from adaptive immune responses. Vaccine candidate strain selection currently involves correlating antigenicity with HA protein sequence among circulating strains, but quantitative comparison of site-specific glycosylation

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14

Taherzadeh, Ghazaleh, Abdollah Dehzangi, Maryam Golchin, Yaoqi Zhou, and Matthew P. Campbell. "SPRINT-Gly: predicting N- and O-linked glycosylation sites of human and mouse proteins by using sequence and predicted structural properties." Bioinformatics 35, no. 20 (2019): 4140–46. http://dx.doi.org/10.1093/bioinformatics/btz215.

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Abstract Motivation Protein glycosylation is one of the most abundant post-translational modifications that plays an important role in immune responses, intercellular signaling, inflammation and host-pathogen interactions. However, due to the poor ionization efficiency and microheterogeneity of glycopeptides identifying glycosylation sites is a challenging task, and there is a demand for computational methods. Here, we constructed the largest dataset of human and mouse glycosylation sites to train deep learning neural networks and support vector machine classifiers to predict N-/O-linked glyco

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15

Hahm, Young Hye, Sung Ho Hahm, Hyoun Young Jo, and Yeong Hee Ahn. "Comparative Glycopeptide Analysis for Protein Glycosylation by Liquid Chromatography and Tandem Mass Spectrometry: Variation in Glycosylation Patterns of Site-Directed Mutagenized Glycoprotein." International Journal of Analytical Chemistry 2018 (September 2, 2018): 1–10. http://dx.doi.org/10.1155/2018/8605021.

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Glycosylation is one of the most important posttranslational modifications for proteins, including therapeutic antibodies, and greatly influences protein physiochemical properties. In this study, glycopeptide mapping of a reference and biosimilar recombinant antibodies (rAbs) was performed using liquid chromatography-electrospray ionization tandem mass spectrometry (LC-ESI-MS/MS) and an automated Glycoproteome Analyzer (GPA) algorithm. The tandem mass analyses for the reference and biosimilar samples indicate that this approach proves to be highly efficient in reproducing consistent analytical

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16

Davis, Nicola J., and Sabine L. Flitsch. "A novel method for the specific glycosylation of proteins." Tetrahedron Letters 32, no. 46 (1991): 6793–96. http://dx.doi.org/10.1016/s0040-4039(00)93605-0.

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17

Chang, Chih-Wei, and Tse-Lok Ho. "A New Glycosylation Method Based on 8-Quinolyl Glycosides." Journal of the Chinese Chemical Society 53, no. 6 (2006): 1567–70. http://dx.doi.org/10.1002/jccs.200600204.

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18

Wakao, Masahiro, Koichi Fukase, and Shoichi Kusumoto. "Novel Molecular Clamp Method for Anomeric Stereocontrol of Glycosylation." Synlett 1999, no. 12 (1999): 1911–14. http://dx.doi.org/10.1055/s-1999-2997.

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19

Niu, Bing, Wencong Lu, Juan Ding, et al. "A two-stage method for O-glycosylation site prediction." Chemometrics and Intelligent Laboratory Systems 108, no. 2 (2011): 142–45. http://dx.doi.org/10.1016/j.chemolab.2011.06.007.

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20

Michalak, Malwina, Martin Simon Kalteis, Aysel Ahadova, et al. "Differential Glycosite Profiling—A Versatile Method to Compare Membrane Glycoproteomes." Molecules 26, no. 12 (2021): 3564. http://dx.doi.org/10.3390/molecules26123564.

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Glycosylation is the most prevalent and varied form of post-translational protein modifications. Protein glycosylation regulates multiple cellular functions, including protein folding, cell adhesion, molecular trafficking and clearance, receptor activation, signal transduction, and endocytosis. In particular, membrane proteins are frequently highly glycosylated, which is both linked to physiological processes and of high relevance in various disease mechanisms. The cellular glycome is increasingly considered to be a therapeutic target. Here we describe a new strategy to compare membrane glycop

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21

Gandolfi-Donadío, Lucía, Carola Gallo-Rodriguez та Rosa M. de Lederkremer. "Facile synthesis of α-D-Araf-(1→5)-D-Galf, the linker unit of the arabinan to the galactan in Mycobacterium tuberculosis". Canadian Journal of Chemistry 84, № 4 (2006): 486–91. http://dx.doi.org/10.1139/v06-025.

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The arabinogalactan is a crucial constituent of the cell wall of mycobacteria. Both monosaccharides (arabinose and galactose) are found in the furanose configuration, absent in mammals. An efficient synthesis of α-D-Araf-(1→5)-D-Galf, the linker unit of the arabinan to the galactan, is described. The strategy relies on the use of a conveniently substituted D-galactono-1,4-lactone as a precursor of the reducing furanose ring. The glycosylation step was performed by the tin(IV) chloride promoted method using 1,2,3,5-tetra-O-benzoyl-α,β-D-arabinofuranose. The arabinose donor was obtained in a cry

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22

Pal, Rita, Anupama Das, and Narayanaswamy Jayaraman. "Radical halogenation-mediated latent–active glycosylations of allyl glycosides." Chemical Communications 54, no. 6 (2018): 588–90. http://dx.doi.org/10.1039/c7cc07332a.

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Radical halogenation-mediated glycosylation using allyl glycosides as donors and as acceptors emerges to be an efficient and hither-to unknown glycosylation method, adhering to the concept of the latent–active methodology.

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23

Ondrušková, Nina, Tomáš Honzík, Jitka Kytnarová, Martin Matoulek, Jiří Zeman, and Hana Hansíková. "Isoelectric Focusing of Serum Apolipoprotein C-III as a Sensitive Screening Method for the Detection of O-glycosylation Disturbances." Prague Medical Report 116, no. 2 (2015): 73–86. http://dx.doi.org/10.14712/23362936.2015.48.

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Apolipoprotein C-III (ApoC-III) is a glycoprotein carrying the most common O-linked glycan structure and is abundantly present in serum, what renders it a suitable marker for analysis of O-glycosylation abnormalities. Isoelectric focusing followed by a Western blot of ApoC-III, using PhastSystem™ Electrophoresis System (GE Healthcare), was introduced as a rather simple and rapid method for screening of certain subtypes of inherited glycosylation disorders. The study’s aim was to establish this method in our laboratory, what included performing the analysis in a group of 170 healthy individuals

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24

De Leoz, Maria Lorna A., David L. Duewer, Adam Fung, et al. "NIST Interlaboratory Study on Glycosylation Analysis of Monoclonal Antibodies: Comparison of Results from Diverse Analytical Methods." Molecular & Cellular Proteomics 19, no. 1 (2019): 11–30. http://dx.doi.org/10.1074/mcp.ra119.001677.

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Glycosylation is a topic of intense current interest in the development of biopharmaceuticals because it is related to drug safety and efficacy. This work describes results of an interlaboratory study on the glycosylation of the Primary Sample (PS) of NISTmAb, a monoclonal antibody reference material. Seventy-six laboratories from industry, university, research, government, and hospital sectors in Europe, North America, Asia, and Australia submitted a total of 103 reports on glycan distributions. The principal objective of this study was to report and compare results for the full range of anal

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25

van Beusekom, Bart, Natasja Wezel, Maarten L. Hekkelman, Anastassis Perrakis, Paul Emsley, and Robbie P. Joosten. "Building and rebuilding N-glycans in protein structure models." Acta Crystallographica Section D Structural Biology 75, no. 4 (2019): 416–25. http://dx.doi.org/10.1107/s2059798319003875.

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N-Glycosylation is one of the most common post-translational modifications and is implicated in, for example, protein folding and interaction with ligands and receptors. N-Glycosylation trees are complex structures of linked carbohydrate residues attached to asparagine residues. While carbohydrates are typically modeled in protein structures, they are often incomplete or have the wrong chemistry. Here, new tools are presented to automatically rebuild existing glycosylation trees, to extend them where possible, and to add new glycosylation trees if they are missing from the model. The method ha

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26

Ramakrishnan, Boopathy, Elizabeth Boeggeman, and Pradman K. Qasba. "Novel Method forin VitroO-Glycosylation of Proteins: Application for Bioconjugation." Bioconjugate Chemistry 18, no. 6 (2007): 1912–18. http://dx.doi.org/10.1021/bc7002346.

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27

Choi, Tae Jin, Ju Yuel Baek, Heung Bae Jeon, and Kwan Soo Kim. "A new efficient glycosylation method employing glycosyl pentenoates and PhSeOTf." Tetrahedron Letters 47, no. 52 (2006): 9191–94. http://dx.doi.org/10.1016/j.tetlet.2006.10.158.

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28

KOCHETKOV, N. K., E. M. KLIMOV, N. N. MALYSHEVA, and A. V. DEMCHENKO. "ChemInform Abstract: A New Stereospecific Method for 1,2-cis-Glycosylation." ChemInform 23, no. 46 (2010): no. http://dx.doi.org/10.1002/chin.199246240.

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29

KOCHETKOV, N. K., E. M. KLIMOV, N. N. MALYSHEVA, and A. V. DEMCHENKO. "ChemInform Abstract: Stereospecific 1,2-cis-Glycosylation: A Modified Thiocyanate Method." ChemInform 23, no. 46 (2010): no. http://dx.doi.org/10.1002/chin.199246261.

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30

Wang, Yali, Hong Zhang, and Wolfgang Voelter. "Block Synthesis of Oligosaccharides under Mild Conditions." Zeitschrift für Naturforschung B 50, no. 4 (1995): 661–66. http://dx.doi.org/10.1515/znb-1995-0431.

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Details on a synthesis of the trisaccharide α-D-Glc(1→6)-β-D-Glc(1→6)-D -Glc are reported. The O-glycosidic linkages were constructed using the sulfoxide glycosylation reaction. This approach proves to be a rapid glycosylation method leading to high yield and good selectivity.

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31

Zhang, Xiaoru, Ruijuan Li, Yuanyuan Chen, Shusheng Zhang, Wenshuang Wang, and Fuchuan Li. "Applying DNA rolling circle amplification in fluorescence imaging of cell surface glycans labeled by a metabolic method." Chemical Science 7, no. 9 (2016): 6182–89. http://dx.doi.org/10.1039/c6sc02089e.

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32

Hipgrave Ederveen, Agnes L., Noortje de Haan, Melissa Baerenfaenger, Dirk J. Lefeber, and Manfred Wuhrer. "Dissecting Total Plasma and Protein-Specific Glycosylation Profiles in Congenital Disorders of Glycosylation." International Journal of Molecular Sciences 21, no. 20 (2020): 7635. http://dx.doi.org/10.3390/ijms21207635.

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Protein N-glycosylation is a multifactorial process involved in many biological processes. A broad range of congenital disorders of glycosylation (CDGs) have been described that feature defects in protein N-glycan biosynthesis. Here, we present insights into the disrupted N-glycosylation of various CDG patients exhibiting defects in the transport of nucleotide sugars, Golgi glycosylation or Golgi trafficking. We studied enzymatically released N-glycans of total plasma proteins and affinity purified immunoglobulin G (IgG) from patients and healthy controls using mass spectrometry (MS). The appl

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33

Hargett, Audra A., Aaron M. Marcella, Huifeng Yu, et al. "Glycosylation States on Intact Proteins Determined by NMR Spectroscopy." Molecules 26, no. 14 (2021): 4308. http://dx.doi.org/10.3390/molecules26144308.

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Protein glycosylation is important in many organisms for proper protein folding, signaling, cell adhesion, protein-protein interactions, and immune responses. Thus, effectively determining the extent of glycosylation in glycoprotein therapeutics is crucial. Up to now, characterizing protein glycosylation has been carried out mostly by liquid chromatography mass spectrometry (LC-MS), which requires careful sample processing, e.g., glycan removal or protein digestion and glycopeptide enrichment. Herein, we introduce an NMR-based method to better characterize intact glycoproteins in natural abund

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34

Shajahan, Asif, Nitin T. Supekar, Han Wu, et al. "Mass Spectrometric Method for the Unambiguous Profiling of Cellular Dynamic Glycosylation." ACS Chemical Biology 15, no. 10 (2020): 2692–701. http://dx.doi.org/10.1021/acschembio.0c00453.

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35

Kim, Soong Hoon, David Augeri, Dan Yang, and Daniel Kahne. "Concise Synthesis of the Calicheamicin Oligosaccharide Using the Sulfoxide Glycosylation Method." Journal of the American Chemical Society 116, no. 5 (1994): 1766–75. http://dx.doi.org/10.1021/ja00084a018.

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36

Schwarz, Flavio, Wei Huang, Cishan Li, et al. "A combined method for producing homogeneous glycoproteins with eukaryotic N-glycosylation." Nature Chemical Biology 6, no. 4 (2010): 264–66. http://dx.doi.org/10.1038/nchembio.314.

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37

Wakao, Masahiro, Koichi Fukase, and Shoichi Kusumoto. "ChemInform Abstract: Novel Molecular Clamp Method for Anomeric Stereocontrol of Glycosylation." ChemInform 31, no. 12 (2010): no. http://dx.doi.org/10.1002/chin.200012234.

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38

Nishida, Yoshihiro, Yuko Shingu, Hirofumi Dohi та Kazukiyo Kobayashi. "One-Pot α-Glycosylation Method Using Appel Agents inN,N-Dimethylformamide". Organic Letters 5, № 14 (2003): 2377–80. http://dx.doi.org/10.1021/ol034269+.

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39

Morzycki, Jacek W., Zenon Łotowski, Leszek Siergiejczyk та ін. "A selective electrochemical method of glycosylation of 3β-hydroxy-Δ5-steroids". Carbohydrate Research 345, № 8 (2010): 1051–55. http://dx.doi.org/10.1016/j.carres.2010.03.018.

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40

Walk, Jordan T., Zachary A. Buchan, and John Montgomery. "Sugar silanes: versatile reagents for stereocontrolled glycosylation via intramolecular aglycone delivery." Chemical Science 6, no. 6 (2015): 3448–53. http://dx.doi.org/10.1039/c5sc00810g.

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41

Ryan, Philip, Andy Hsien Wei Koh, Anna Elizabeth Lohning, and Santosh Rudrawar. "Solid-Phase O-Glycosylation with a Glucosamine Derivative for the Synthesis of a Glycopeptide." Australian Journal of Chemistry 70, no. 10 (2017): 1151. http://dx.doi.org/10.1071/ch17201.

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An efficient synthesis of the O-linked glycosylamino acid Fmoc–l-Ser((Ac)3–β-d-GlcNAc)-OH building block is described. The utility of the method was demonstrated with direct solid-phase O-glycosylation of the hydroxyl group on the amino acid (Ser) side chain of a human α-A crystallin-derived peptide (AIPVSREEK) in nearly quantitative glycosylation yield.

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42

Olczak, Mariusz, and Bożena Szulc. "Modified secreted alkaline phosphatase as an improved reporter protein for N-glycosylation analysis." PLOS ONE 16, no. 5 (2021): e0251805. http://dx.doi.org/10.1371/journal.pone.0251805.

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N-glycosylation is a common posttranslational modification of proteins in eukaryotic cells. The modification is often analyzed in cells which are able to produce extracellular, glycosylated proteins. Here we report an improved method of the use of genetically modified, secreted alkaline phosphatase (SEAP) as a reporter glycoprotein which may be used for glycoanalysis. Additional N-glycosylation sites introduced by site-directed mutagenesis significantly increased secretion of the protein. An improved purification protocol of recombinant SEAP from serum or serum-free media is also proposed. The

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43

Ghosh, Titli, Ananya Mukherji, Hemant Kumar Srivastava, and Pavan K. Kancharla. "Secondary amine salt catalyzed controlled activation of 2-deoxy sugar lactols towards alpha-selective dehydrative glycosylation." Organic & Biomolecular Chemistry 16, no. 16 (2018): 2870–75. http://dx.doi.org/10.1039/c8ob00423d.

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44

Wolters-Eisfeld, Gerrit, Baris Mercanoglu, Alina Strohmaier, Cenap Guengoer, Jakob R. Izbicki, and Maximilian Bockhorn. "Hypoxia induced HIF1a-mediated O-GalNAc glycosylation of cytosolic O-GlcNAcylated proteins to regulate signaling pathways in pancreatic cancer." Journal of Clinical Oncology 35, no. 15_suppl (2017): e15739-e15739. http://dx.doi.org/10.1200/jco.2017.35.15_suppl.e15739.

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e15739 Background: Hypoxia induced reprogramming of cell energy metabolism and changes in glycosylation are hallmarks of cancer promoting the induction of an invasive and treatment-resistant phenotype, triggering metastases at an early stage of tumor development. We examined the impact of hypoxia on O-GalNAc glycosylation in human HEK293, PDAC cell lines and clinical specimens. Methods: We profiled the expression of 88 glycosylation related genes by qPCR in HEK293 cells subjected to hypoxia either induced by 1% O2 or 200 mm CoCl2 identifying key O-GalNAc glycosyltransferases downregulated. Fun

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45

Yadav, Sharda, Laura G. Carrascosa, Abu A. I. Sina, Muhammad J. A. Shiddiky, Michelle M. Hill, and Matt Trau. "Electrochemical detection of protein glycosylation using lectin and protein–gold affinity interactions." Analyst 141, no. 8 (2016): 2356–61. http://dx.doi.org/10.1039/c6an00528d.

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46

Mi, Jianing, Kun-Peng Jia, Aparna Balakrishna, Jian You Wang, and Salim Al-Babili. "An LC-MS profiling method reveals a route for apocarotene glycosylation and shows its induction by high light stress in Arabidopsis." Analyst 144, no. 4 (2019): 1197–204. http://dx.doi.org/10.1039/c8an02143k.

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47

Nagy, A., K. Marciniak-Darmochwał, S. Krawczuk, D. Mierzejewska, H. Kostyra, and É. Gelencsér. "Influence of glycation and pepsin hydrolysis on immunoreactivity of albumin/globulin fraction of herbicide resistant wheat line." Czech Journal of Food Sciences 27, No. 5 (2009): 320–29. http://dx.doi.org/10.17221/48/2008-cjfs.

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The aim of this study was to investigate the influence of non-enzymatic glycosylation on the immunogenic properties of soluble wheat proteins. Albumin/globulin fractions of herbicide resistant wheat line were non-enzymatically glycosylated using glucose for seven days at 37°C. The changes in their structures and immunoreactivity were then determined. The protein fractions were also hydrolysed with pepsin to determine the resistance to digestion. Albumin/globulin fractions before and after non-enzymatic glycosylation were analysed using <i>o</i>-phthaldialdehyde method and sodium do

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48

Xu, Tingting, and Xueming Wu. "Preparative separation of mangiferin glycosides by high speed counter current chromatography and comparison of their antioxidant and antitumor activities." RSC Advances 10, no. 43 (2020): 25780–85. http://dx.doi.org/10.1039/d0ra04307a.

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49

Wu, Ren, Meixian Zhou, and Hui Wu. "Purification and Characterization of an Active N-Acetylglucosaminyltransferase Enzyme Complex from Streptococci." Applied and Environmental Microbiology 76, no. 24 (2010): 7966–71. http://dx.doi.org/10.1128/aem.01434-10.

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ABSTRACT A new family of bacterial serine-rich repeat glycoproteins can function as adhesins required for biofilm formation and pathogenesis in streptococci and staphylococci. Biogenesis of these proteins depends on a gene cluster coding for glycosyltransferases and accessory secretion proteins. Previous studies show that Fap1, a member of this family from Streptococcus parasanguinis, can be glycosylated by a protein glycosylation complex in a recombinant heterogeneous host. Here we report a tandem affinity purification (TAP) approach used to isolate and study protein complexes from native str

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Zhang, Jianbo, Youxian Dong, Madina Yuma, et al. "Copper-Catalyzed Stereoselective Synthesis of 2-Deoxygalactosides." Synlett 31, no. 11 (2020): 1087–93. http://dx.doi.org/10.1055/s-0040-1707098.

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Abstract:

An efficient glycosylation method to synthesize 2-deoxy-O-galactosides based on a Cu(II)-catalyzed reaction without additional ligand has been developed. The glycosylation was amenable to different protected glycal donors and a wide range of acceptors including alcohols, amino acids, sugars, and phenol, and proceeds with excellent yield and high α-selectivity under mild conditions. The reaction proceeds readily on a gram scale, and its versatility is exemplified in the synthesis of oligosaccharides.

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