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Biogenic Synthesis of Nanoparticulate Materials for Antiviral Applications
Published in Devarajan Thangadurai, Saher Islam, Charles Oluwaseun Adetunji, Viral and Antiviral Nanomaterials, 2022
Kah Hon Leong, Jit Jang Ng, Lan Ching Sim, Pichiah Saravanan, Chaomeng Dai, Bo Tan
This assessment is to detect the virus entry into any specimen. It can hydrolyze the β-glycosidic bond between the galactose and its organic portion can be hydrolyze thru exoglycosidase. This is vital for the organisms as it provides energy and carbon basis through the interruption of lactose into galactose and glucose (Yin et al. 2017). Therefore, it uses as a reporter gene to evaluate the expression level in the host cell, where it delivers indirect indication for the capability of nanoparticles treatment in treating the virus infection.
Carbohydrate Histochemistry
Published in Joan Gil, Models of Lung Disease, 2020
Bradley A. Schulte, Russell A. Harley, Samuel S. Spicer
Loss of staining after digestion with a specific glycosidase yields information about the location of the sugar hydrolyzed by the enzyme. Moreover, lectin histochemical methods make it possible to determine the location of a given sugar with a specific enzyme digestion by imparting lectin staining for the specific penultimate sugar or sugar sequence exposed after the digestion. Most sialoglyco-conjugates, for example, contain galactose or N-acetylgalactosamine penultimate to the terminal sialic acid and gain reactivity for peanut lectin (Steward et al., 1980; Schulte and Spicer, 1985) or a lectin from Dolichos biflorus (Schulte and Spicer, 1985; Schulte et al., 1985a), respectively, after enzymatic removal of the sialic acid. It is conceivable, that a combination of digestion with one or another specific exoglycosidase to remove the terminal sugars in an oligosaccharide chain at a precise location, followed by a battery of lectin procedures to identify the sugar rendered terminal by digestion, could be performed repeatedly to yield information about the sequence of sugars in the oligosaccharide chains.
The “less-is-more” in therapeutic antibodies: Afucosylated anti-cancer antibodies with enhanced antibody-dependent cellular cytotoxicity
Published in mAbs, 2018
Natasha A. Pereira, Kah Fai Chan, Pao Chun Lin, Zhiwei Song
Chemoenzymatic remodelling of antibodies represents another strategy for generating afucosylated antibodies. This chemical biology approach involves the use of an endo-β-N-acetylglucosamidase such as Endo S to remove the majority of N-glycans from antibodies, followed by treatment with an exoglycosidase such as fucosidase to remove the core fucose. The mono-GlcNac is then further extended by transglycosylation with Endo S-based glycosynthases in the presence of desialylated complex type glycan oxazoline, which serve as donor substrates to generate different homogenous afucosylated glycoforms.100 However, this method is not cost effective for producing afucosylated therapeutic antibodies.
Human disease glycomics: technology advances enabling protein glycosylation analysis – part 1
Published in Expert Review of Proteomics, 2018
Arun V Everest-Dass, Edward S X Moh, Christopher Ashwood, Abdulrahman M M Shathili, Nicolle H Packer
High isomeric selectivity can be obtained in CE analysis of fluorescently labeled glycans through the use of borate buffer that complexes with glycans. In noncomplexing buffers, the separation is usually attributed to size, charge, and to a lesser extent the shape of the glycan moiety [105]. Glycan peaks from CE are usually identified by (a) correlation of retention time with Glc units of a maltose ladder as reference; (b) comparison with glycan standards; (c) structure deduction through a series of exoglycosidase digestions; and (d) by coupling with detectors such as that used in DNA sequencers, laser-induced fluorescence (LIF) and MS [105].
Impact of Fc N-glycan sialylation on IgG structure
Published in mAbs, 2019
Zhongqi Zhang, Bhavana Shah, Jason Richardson
Figure 3 shows the SIC of sialylated glycopeptides, after tryptic digestion of the four IgG antibodies for 24 h under a native-like condition. It has been shown previously that after 24 h of digestion the CH2-domain glycopeptides are nearly fully released, as the glycoform profile is similar to that from a full digestion.5,13 As described below, glycoforms were identified based on a combination of evidences, including the glycan profiles determined from HILIC-MS/MS analysis of released glycans, exoglycosidase digestion, as well as the order of elution.