A selective method for sequential splitting of O- and N-linked glycans from N,O-glycoproteins

Likhosherstov, L. M.; Новикова, О. С.; Derevitskaya, V. A.; Kochetkov, Nikolay K.

doi:10.1016/0008-6215(90)84093-a

Cited by 34 publications

(27 citation statements)

References 11 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…To overcome this limitation, the sample could be treated with peptide N-glycosidase F in order to recover the N-linked oligosaccharides, followed by ␤-elimination of the glycoprotein to recover the O-linked oligosaccharides. Other methods have been suggested for doing selective release of N-linked and O-linked glycans using hydrazinolysis (3) under different conditions or using alkaline elimination with reducing agents in combination with additional inorganic salts (18).…”

Section: Discussionmentioning

confidence: 99%

Analysis of O-Linked Reducing Oligosaccharides Released by an In-line Flow System

Karlsson¹,

Packer²

2002

Analytical Biochemistry

View full text Add to dashboard Cite

Section: Discussionmentioning

confidence: 99%

Analysis of O-Linked Reducing Oligosaccharides Released by an In-line Flow System

Karlsson¹,

Packer²

2002

Analytical Biochemistry

View full text Add to dashboard Cite

“…DCC (Aldrich) was purchased. α-L-Rhamnopyranosylamine and β-D-lactosylamine were prepared by the literature methods [6,8] in 80-82% purity and were used without further purification.…”

Section: Methodsmentioning

confidence: 99%

“…The triterpene parts of the 13 C NMR spectra of 2, 3, and 6 were identical to those of the starting 3-O-acylates [4]. Signals in the 13 C NMR spectra of newly synthesized N-glycoconjugates were assigned based on literature data for glycyrrhetic acid derivatives [4,5] and starting β-glycosylamines [6][7][8]. The CSs of C8 and C14 were defined more accurately using our published 1 H and 13 C high-resolution spectra (600 and 125 MHz) for glycyrrhizic acid and its derivatives [9].…”

mentioning

confidence: 99%

Synthesis of N-glycoconjugates of glycyrrhetic acid

et al. 2006

View full text Add to dashboard Cite

“…They can be prepared via reduction of an anomeric azide [118][119][120] precursor that has already been extended with different saccharides. Unprotected saccharides can be converted to anomeric glycosyl amines by treatment with a saturated solution of ammonium hydrogen carbonate (Kochetkov method) [122,123]. Unprotected saccharides can be converted to anomeric glycosyl amines by treatment with a saturated solution of ammonium hydrogen carbonate (Kochetkov method) [122,123].…”

Section: Synthesis Of N-glycopeptidesmentioning

confidence: 99%

Advances inN‐ andO‐Glycopeptide Synthesis – A Tool to Study Glycosylation and Develop New Therapeutics

Westerlind

Kunz

2011

Amino Acids, Peptides and Proteins in Organic Chemistry

View full text Add to dashboard Cite

Many proteins are co-or post-translationally modified by mono-or oligosaccharides. It has become evident that these glycoproteins play important roles in diverse biochemical processes. The saccharides contribute with physiochemical properties, which include conformational effects on the protein, stability to proteolysis, and lubrication of cells. In addition, the glycans are involved in cell-cell recognition and cell-external agent interactions. These interactions induce biological events, which include cell growth and differentiation, cell proliferation, cell adhesion, binding of pathogens, fertilization, and immune responses [1-6]. The glycans assist in protein folding and transport, and they are involved in pathogenic processes like chronic inflammation [5], viral and bacterial infections [7-10], tumor growth and metastasis [11,12], and autoimmune disorders [13,14]. The variety of events affected by protein glycosylation is not surprising. Carbohydrates are unique in their structural complexity and, in contrast to oligonucleotides and proteins, they can be connected in more than one form: connected via different configural positions of the glycan residue and also via an anomeric aor b-glycosidic linkage. The different modes of connection can lead to long linear or highly branched saccharide structures. By combining different types of glycans like galactose, glucose, N-acetyl galactosamine (GalNAc), N-acetyl glucosamine (GlcNAc), fucose, mannose, sialic acid, and others, an enormous amount of combinations can be formed. Nature only uses a small portion of these possible combinations. The biosyntheses of different oligosaccharides are dependent of glycosyltransferases, which are gene-encoded. Each type of connection and glycan residue needs a specific enzyme, and for practical reasons this restricts the number of combinations. Nature also limits the number of final products that can be made by having common core structures. The saccharides can be linked to the protein backbone via an O-glycosidic bond or via amide bond formation in N-glycoproteins. In the most common type of O-glycoproteins, the mucin type, a GalNAc residue is connected to the protein backbone via an O-glycosidic linkage to serine or threonine [15,16]. The GalNAc residue can be further extended with

show abstract

A selective method for sequential splitting of O- and N-linked glycans from N,O-glycoproteins

Cited by 34 publications

References 11 publications

Analysis of O-Linked Reducing Oligosaccharides Released by an In-line Flow System

Analysis of O-Linked Reducing Oligosaccharides Released by an In-line Flow System

Synthesis of N-glycoconjugates of glycyrrhetic acid

Advances inN‐ andO‐Glycopeptide Synthesis – A Tool to Study Glycosylation and Develop New Therapeutics

Contact Info

Product

Resources

About