1987
DOI: 10.1021/bi00378a023
|View full text |Cite
|
Sign up to set email alerts
|

Comparative structural study of the N-linked oligosaccharides of human normal and pathological immunoglobulin G

Abstract: The structures of oligosaccharides of normal and pathological immunoglobulin G (IgG) are reported. Asparagine-linked neutral oligosaccharides were released by N-oligosaccharide glycopeptidase (almond) digestion. The reducing ends of the oligosaccharide chains thus obtained were aminated with a fluorescent reagent, 2-aminopyridine, and the mixture of pyridylamino derivatives of the oligosaccharides was separated by reverse-phase high-performance liquid chromatography. It was possible to separate 15 out of the 1… Show more

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
2
2
1

Citation Types

6
116
0

Year Published

1989
1989
2017
2017

Publication Types

Select...
8

Relationship

1
7

Authors

Journals

citations
Cited by 170 publications
(122 citation statements)
references
References 23 publications
6
116
0
Order By: Relevance
“…Sequential digestion of N2 oligosaccharide released two galactose residues with @-galactosidase, two GlcNAc residues with @-N-acetylglucosaminidase, two mannose residues with a-mannosidase, and one mannose residue with @-mannosidase (Table 3). The values of chemical shifts of N2 agreed with those of the pyridylamino derivatives of oligosaccharide H from human IgG [23] and oligosaccharide E from urinary erythropoietin [24] (Table 4). Accordingly, the structure of N2 was proposed as that of (3) in Fig.…”
Section: Structures Of the Neutral Chainssupporting
confidence: 53%
See 1 more Smart Citation
“…Sequential digestion of N2 oligosaccharide released two galactose residues with @-galactosidase, two GlcNAc residues with @-N-acetylglucosaminidase, two mannose residues with a-mannosidase, and one mannose residue with @-mannosidase (Table 3). The values of chemical shifts of N2 agreed with those of the pyridylamino derivatives of oligosaccharide H from human IgG [23] and oligosaccharide E from urinary erythropoietin [24] (Table 4). Accordingly, the structure of N2 was proposed as that of (3) in Fig.…”
Section: Structures Of the Neutral Chainssupporting
confidence: 53%
“…Jvalues are shown in the angled brackets. IgG-E results are from [23] The idcntity of the peaks eluted within 20 min from octadccylsilane (Fig. 8C) is unclear.…”
Section: Structure Of the Core Regionsmentioning
confidence: 99%
“…Notably under these conditions, which also have been used for defucosylation of bromelain and peroxidase, most of the fucose, which is a1 6 linked to Asn-GlcNAc in IgG [31], was retained ( Table 3). The tryptic human IgG glycopeptide was isolated the same way as BrlPep except that DEAE-Sephadex A25 was used.…”
Section: Human Igg Glycopeptidementioning
confidence: 99%
“…A tryptic glycopeptide from human IgG, containing fucose a1 -+6 linked to Asn-GlcNAc [31], was chosen to compare the enzymatic activities of PNGase A and PNGase F with a substrate of mammalian origin. For both enzymes, human IgG glycopeptide was the best substrate among those employed (Fig.…”
Section: Pngase Digestion O J a Glycopeptide From Human Iggmentioning
confidence: 99%
“…Another study (20) was theˆrst to show the diŠer-ences between normal and pathological human IgG oligosaccharides by using HPLC.…”
Section: C-1 Human Igg N-glycansmentioning
confidence: 99%