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相关概念视频

Oligosaccharide Assembly01:24

Oligosaccharide Assembly

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Protein glycosylation starts in the ER lumen and continues in the Golgi apparatus. Glycosyltransferases catalyze the addition of sugar molecules or glycosylation of proteins. Usually, these enzymes add sugars to the hydroxyl groups of selected serine or threonine residues to form O-linked glycans or the amino groups of asparagine residues to form N-linked glycans. Different positions on the same polypeptide chain can contain differently linked glycans.
Multiple sugar molecules that may or may...
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Proteoglycans01:05

Proteoglycans

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Glycans, a class of complex heterogeneous molecules, can be covalently attached to proteins to form glycosylated proteins that regulate various physiological and pathological processes. Glycosylated proteins or glycoproteins comprise N-linked and O-linked oligosaccharides. O-glycosylation is the most common type of protein glycosylation. Here, glycans attach to the oxygen atom of the hydroxyl groups of Serine or Threonine residues. O-linked glycosylation occurs later in protein processing,...
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Oral Hypoglycemic Agents: α-Glucosidase Inhibitors01:19

Oral Hypoglycemic Agents: α-Glucosidase Inhibitors

205
α-glucosidase inhibitors, including acarbose (Precose), miglitol (Glyset), and voglibose (Voglib) (primarily available in Asia), are drugs that control blood sugar levels by delaying the digestion of starch and disaccharides. They achieve this by inhibiting α-glucosidase enzymes in the intestine, which slow the absorption of carbohydrates in the intestine, which in turn leads to a prolonged release of the glucoregulatory hormone GLP-1 from intestinal L-cells.
Acarbose and miglitol are...
205
Protein Glycosylation01:25

Protein Glycosylation

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Glycosylation, the most common post-translational modification for proteins, serves diverse functions. Adding sugars to proteins makes the proteins more resistant to proteolytic digestion. Glycosylated proteins can act as markers and receptors to promote cell-cell adhesion. Additionally, they have many essential quality control functions in the cell, such as correct protein folding and facilitating transport of misfolded proteins to the cytosol, which can be degraded.
Glycosylation occurs in...
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Allergic Reactions02:06

Allergic Reactions

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Overview
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Glycosaminoglycans01:23

Glycosaminoglycans

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Glycosaminoglycans (GAGs), also known as mucopolysaccharides, are long and linear polymers comprising of specific repeating disaccharides - the amino sugar that can be N-acetylglucosamine or N-acetylgalactosamine, and a uronic acid that is usually glucuronic acid or iduronic acid.
GAGS are found in the extracellular matrix of vertebrates, invertebrates, and bacteria. Due to their polar nature they attract water, and serve as excellent lubricants or shock absorbers in an animal body.
Hyaluronic...
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相关实验视频

Updated: Jul 17, 2025

Determination of Glucan Chain Length Distribution of Glycogen Using the Fluorophore-Assisted Carbohydrate Electrophoresis FACE Method
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Determination of Glucan Chain Length Distribution of Glycogen Using the Fluorophore-Assisted Carbohydrate Electrophoresis FACE Method

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通过糖化降低Ara h 2的过敏性是通过减少糖链长度和同位素来确定的.

Ping Yang1, Xumei Wang2, Hui Wang1

  • 1State Key Laboratory of Food Science and Resources, Nanchang University, Nanchang, Jiangxi 330047, China.

Food chemistry
|September 2, 2023
PubMed
概括

减少糖链长度和异构体显著影响花生过敏原 Ara h 2 过敏性在糖化后. 核糖和银河糖通过改变Ara h 2结构有效降低过敏性,有助于低过敏性产品的开发.

关键词:
过敏性 过敏性 过敏性时间 h 2 2 时间葡萄糖化是指糖化的一种方式.在HPLC-HCD-MS/MS中使用.这些同位素是异构体.减少糖链长度 减少糖链长度

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Analysis of N-glycans from Raphanus sativus Cultivars Using PNGase H+
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Analysis of N-glycans from Raphanus sativus Cultivars Using PNGase H+

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Sequencing of Plant Wall Heteroxylans Using Enzymic, Chemical Methylation and Physical Mass Spectrometry, Nuclear Magnetic Resonance Techniques
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相关实验视频

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Analysis of N-glycans from Raphanus sativus Cultivars Using PNGase H+
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Sequencing of Plant Wall Heteroxylans Using Enzymic, Chemical Methylation and Physical Mass Spectrometry, Nuclear Magnetic Resonance Techniques
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科学领域:

  • 食物过敏研究 食物过敏研究
  • 葡萄糖生物学 葡萄糖生物学
  • 蛋白质化学 蛋白质化学

背景情况:

  • 花生过敏是一个重要的健康问题,花生2是主要的过敏原.
  • 糖化,糖和蛋白质之间的非酶反应,可以改变蛋白质的结构和功能.
  • 了解不同降解糖如何影响过敏性对于开发低过敏性食品至关重要.

研究的目的:

  • 为了研究减少糖链长度和同位素对花生蛋白 Ara h 2 在糖化后的过敏性的影响.
  • 阐明与各种糖的糖化改变Ara h 2过敏性的机制.
  • 为选择最佳的降解糖来制造低过敏的花生产品提供理论基础.

主要方法:

  • 净化Ara h 2的糖化与不同的降解糖 (ribose, galactose及其同位素).
  • 分析基化位点和修改后的植物的形状/线性表位变化. 2.
  • 评估由此产生的糖化结合物的过敏性.

主要成果:

  • 阿拉希2显示出更高的敏感性与短链糖,如糖.
  • 与其异构体相比,银糖糖化导致更多的糖化位点,可能是由于立体化学差异.
  • 亚二糖结合物表现出最低的过敏性,表明显著减少.
  • Galactose 在减少 Ara h 2 的过敏性方面比其同位素更有效,这归因于其末端化基组的固体效应.
  • 糖化与核糖导致了对形状表位的大量破坏和对 Ara h 2 上线性表位的掩盖.

结论:

  • 降低糖的结构,包括链条长度和异构体配置,极大地影响了Ara h 2的糖化和随后的过敏性降低.
  • 短链糖,如核糖和特定的配置,如银河糖更有效地减少Ara h 2过敏性.
  • 糖化通过破坏关键的过敏原表位物来修改Ara h 2,为开发低过敏原花生成分提供了可行的策略.