scholarly journals Structure of carbohydrate unit A or porcine thyroglobulin

1981 ◽  
Vol 195 (3) ◽  
pp. 691-699 ◽  
Author(s):  
T Tsuji ◽  
K Yamamoto ◽  
T Irimura ◽  
T Osawa
Keyword(s):  
Column Chromatography ◽  
Core Structure ◽  
Methylation Analysis ◽  
Complex Type ◽  
Form Complex ◽  
Sugar Chains ◽  
Carbohydrate Unit ◽  
Terminal Mannose

The unit A-type glycopeptides were purified from porcine thyroglobulin by Pronase digestion followed by chromatography on a DEAE-Sephadex A-25 column. These glycopeptides were separated into five fractions (UA-I, -II, -IV and -V) by Dowex 50W (X2) column chromatography. Fractions UA-I, -II, -III, -IV and -V were found to have the compositions (Man)9(GlcNAc)2-Asn, (Man)8(GlcNAc)2-Asn, (Man)7(GlcNAc)2-Asn, (Man)6(GlcNAc)2-Asn and (Man)5(GlcNAc)2-Asn respectively. The structures of these five fractions were investigated by the combination of exo- and endo-glycosidase digestions, methylation analysis. Smith periodate degradation and acetolysis. The results showed that fraction UA-V had the simplest structure: see formula in text. The larger glycopeptides (fractions UA-I, -II, -III and -IV) contained additional mannose residues alpha (1 leads to 2)-linked to the terminal mannose residues in the above core structure. These unit A-type glycopeptides appear to be biosynthetic intermediates that are to be processed to form complex-type glycopeptides (unit B-type sugar chains).

scholarly journals The structure of carbohydrate unit B of porcine thyroglobulin

1981 ◽  
Vol 195 (3) ◽  
pp. 701-713 ◽  
Author(s):  
K Yamamoto ◽  
T Tsuji ◽  
T Irimura ◽  
T Osawa
Keyword(s):  
Sialic Acid ◽  
Concanavalin A ◽  
Deae Cellulose ◽  
Structural Features ◽  
The Other ◽  
Methylation Analysis ◽  
Complex Type ◽  
Mannose Residue ◽  
Sugar Chains ◽  
Carbohydrate Unit

The oligosaccharide fraction was obtained from porcine thyroglobulin by hydrazinolysis. Four fractions of unit B-type oligosaccharides were purified by successive chromatographies on columns of DEAE-cellulose and concanavalin A-Sepharose, and their structures were investigated by the combination of endo- and exo-glycosidase digestions, methylation analysis and Smith degradation. From the results of these studies, the structures of the unit B oligosaccharides were proposed to be as follows: see formula in text. Thus the glycoprotein was found to have triantennary and biantennary complex-type oligosaccharides as acidic sugar chains. Concerning the triantennary oligosaccharides, the following structural features were shown: (1) the sialic acid residues were not localized on certain specific branches but distributed on all three branches; (2) however, alpha (2 leads to 3)-linked sialic acid residues were exclusively located on the terminal of the branch arising from C-4 of the branching alpha-mannose residue, whereas alpha (2 leads to 6)-linked sialic acid residues occupied terminals of the other branches; (3) the outer branching alpha-mannose residue was attached to C-3 or C-6 of an inner branching beta-linked mannose residue, and both types were observed to exist.

scholarly journals Carbohydrate structure of human pancreatic elastase 1

1991 ◽  
Vol 278 (2) ◽  
pp. 505-514 ◽  
Author(s):  
P Wendorf ◽  
D Linder ◽  
A Sziegoleit ◽  
R Geyer
Keyword(s):  
Gel Filtration ◽  
Methylation Analysis ◽  
Complex Type ◽  
Pancreatic Elastase ◽  
Blood Group A ◽  
Elastase 1 ◽  
Glycosylation Sites ◽  
Group A ◽  
Sugar Chains ◽  
Pancreatic Elastase 1

Human pancreatic elastase 1 (E1) is a glycoprotein containing two potential N-glycosylation sites, one of which carries a carbohydrate moiety [Wendorf, Geyer, Sziegoleit & Linder (1989) FEBS Lett. 249, 275-278]. In order to study its glycosylation, glycoprotein isolated from post-mortem pancreas tissue of 75 donors was digested with trypsin. Oligosaccharides were liberated from resulting glycopeptides by treatment with peptide-N4-(N-acetyl-beta-glycosaminyl)-asparagine amidase F, radiolabelled by reduction with KB3H4 and separated by h.p.l.c. and gel filtration. Major oligosaccharide alditol fractions, representing 67.8 mol% of total glycans, were characterized by methylation analysis and sequential degradation with exoglycosidases. The results revealed that about two-fifths of the partially truncated, mainly biantennary, complex-type glycans found comprised blood group A, B, Lea (or X), difucosyl A or difucosyl B determinants, which could be assigned to lactosamine antennae linked to Man(alpha 1-3)- residues of the sugar chains.

scholarly journals Structures of the asparagine-linked oligosaccharides of guinea-pig factor B of the alternative complement pathway

1990 ◽  
Vol 272 (2) ◽  
pp. 533-535 ◽  
Author(s):  
T Mizuochi ◽  
J Hamako ◽  
K Titani ◽  
M Matsushita ◽  
H Okada
Keyword(s):  
Guinea Pig ◽  
Column Chromatography ◽  
Paper Electrophoresis ◽  
Alternative Complement Pathway ◽  
Complement Pathway ◽  
Methylation Analysis ◽  
Complex Type ◽  
Factor B ◽  
Alternative Complement

This paper describes the structures of the asparagine-linked oligosaccharides of two forms of guinea-pig Factor B of the alternative complement pathway with different Mr values. Oligosaccharides were quantitatively liberated from both glycoproteins by hydrazinolysis, fractionated by paper electrophoresis and Bio-Gel P-4 column chromatography, and their structures determined by sequential exoglycosidase digestions in conjunction with methylation analysis. Both glycoproteins were shown to have the same biantennary complex-type oligosaccharides but it is suggested that they contain different numbers of oligosaccharide chains.

scholarly journals O-methylated N-glycans Distinguish Mosses from Vascular Plants

Biomolecules ◽  
2022 ◽  
Vol 12 (1) ◽  
pp. 136
Author(s):  
David Stenitzer ◽  
Réka Mócsai ◽  
Harald Zechmeister ◽  
Ralf Reski ◽  
Eva L. Decker ◽  
...  
Keyword(s):  
Green Algae ◽  
Vascular Plants ◽  
Land Plants ◽  
Phylogenetic Relation ◽  
Complex Type ◽  
Animal Kingdom ◽  
Moss Species ◽  
First Finding ◽  
The Common ◽  
Terminal Mannose

In the animal kingdom, a stunning variety of N-glycan structures have emerged with phylogenetic specificities of various kinds. In the plant kingdom, however, N-glycosylation appears to be strictly conservative and uniform. From mosses to all kinds of gymno- and angiosperms, land plants mainly express structures with the common pentasaccharide core substituted with xylose, core α1,3-fucose, maybe terminal GlcNAc residues and Lewis A determinants. In contrast, green algae biosynthesise unique and unusual N-glycan structures with uncommon monosaccharides, a plethora of different structures and various kinds of O-methylation. Mosses, a group of plants that are separated by at least 400 million years of evolution from vascular plants, have hitherto been seen as harbouring an N-glycosylation machinery identical to that of vascular plants. To challenge this view, we analysed the N-glycomes of several moss species using MALDI-TOF/TOF, PGC-MS/MS and GC-MS. While all species contained the plant-typical heptasaccharide with no, one or two terminal GlcNAc residues (MMXF, MGnXF and GnGnXF, respectively), many species exhibited MS signals with 14.02 Da increments as characteristic for O-methylation. Throughout all analysed moss N-glycans, the level of methylation differed strongly even within the same family. In some species, methylated glycans dominated, while others had no methylation at all. GC-MS revealed the main glycan from Funaria hygrometrica to contain 2,6-O-methylated terminal mannose. Some mosses additionally presented very large, likewise methylated complex-type N-glycans. This first finding of the methylation of N-glycans in land plants mirrors the presumable phylogenetic relation of mosses to green algae, where the O-methylation of mannose and many other monosaccharides is a common trait.

Microbial Endo-β-N-Acetylglucosaminidases Acting on Complex-Type Sugar Chains of Glycoproteins

1991 ◽  
Vol 110 (1) ◽  
pp. 17-21 ◽  
Author(s):  
Setsu Kadowaki ◽  
Kenji Yamamoto ◽  
Masatoki Fujisaki ◽  
Tatsurokuro Tochikura
Keyword(s):  
Complex Type ◽  
Sugar Chains

Complexity of type IV collagens: from network assembly to function

2019 ◽  
Vol 400 (5) ◽  
pp. 565-574 ◽  
Author(s):  
Yuexin Wu ◽  
Gaoxiang Ge
Keyword(s):  
Type Iv Collagen ◽  
Network Formation ◽  
Basement Membranes ◽  
Structural Components ◽  
Collagen Network ◽  
Complex Type ◽  
Form Complex ◽  
Structural Support ◽  
Type Iv ◽  
Covalent Crosslinking

Abstract Collagens form complex networks in the extracellular space that provide structural support and signaling cues to cells. Network-forming type IV collagens are the key structural components of basement membranes. In this review, we discuss how the complexity of type IV collagen networks is established, focusing on collagen α chain selection in type IV collagen protomer and network formation; covalent crosslinking in type IV collagen network stabilization; and the differences between solid-state type IV collagen in the extracellular matrix and soluble type IV collagen fragments. We further discuss how complex type IV collagen networks exert their physiological and pathological functions through cell surface integrin and nonintegrin receptors.

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