Skip to main content

Lund University Publications

LUND UNIVERSITY LIBRARIES

Location and characterization of the three carbohydrate prosthetic groups of human protein HC

Escribano, J ; Lopex-Otin, C ; Hjerpe, A ; Grubb, A LU orcid and Mendez, E (1990) In FEBS Letters 266(1-2). p.167-170
Abstract

Three different carbohydrate prosthetic groups associated to three chymotryptic peptides, Q1, Q2 and Q3, were isolated from the reduced and carboxymethylated human protein HC. The first oligosaccharide forms an O-glycosidic linkage with a threonine residue at position 5 in the polypeptide chain of protein HC. The second and third carbohydrate prosthetic groups form N-linkages with asparagine residues at positions 17 and 96. Oligosaccharides present in Q1 contain 1 residue of NANA, 2 of GalNAc and 1 of Gal corresponding to the following structure: -O-GalNAc-GalNAc-Gal-NANA. Q2 contains 3 NANA, 9 GlcNAc, 2 Gal and 3 Man, and Q3 contains 2 NANA, 5 GlcNAc, 1 Gal and 2 Man. The sugar compositions of Q2 and Q3 oligosaccharides are compatible... (More)

Three different carbohydrate prosthetic groups associated to three chymotryptic peptides, Q1, Q2 and Q3, were isolated from the reduced and carboxymethylated human protein HC. The first oligosaccharide forms an O-glycosidic linkage with a threonine residue at position 5 in the polypeptide chain of protein HC. The second and third carbohydrate prosthetic groups form N-linkages with asparagine residues at positions 17 and 96. Oligosaccharides present in Q1 contain 1 residue of NANA, 2 of GalNAc and 1 of Gal corresponding to the following structure: -O-GalNAc-GalNAc-Gal-NANA. Q2 contains 3 NANA, 9 GlcNAc, 2 Gal and 3 Man, and Q3 contains 2 NANA, 5 GlcNAc, 1 Gal and 2 Man. The sugar compositions of Q2 and Q3 oligosaccharides are compatible with that of the complex kind. The amount of oligosaccharides present in Q1, Q2 and Q3 corresponded respectively to 3.0%, 12.2% and 7.3% of the weight of protein HC. No difference was found between the carbohydrate composition of urinary and plasma protein HC.

(Less)
Please use this url to cite or link to this publication:
author
; ; ; and
publishing date
type
Contribution to journal
publication status
published
keywords
Alpha-Globulins/ultrastructure, Amino Acid Sequence, Amino Acids/analysis, Carbohydrates/analysis, Chromatography, High Pressure Liquid, Glycoproteins/ultrastructure, Humans, Molecular Sequence Data, Peptide Fragments/analysis
in
FEBS Letters
volume
266
issue
1-2
pages
167 - 170
publisher
Wiley-Blackwell
external identifiers
  • scopus:0025344805
  • pmid:1694784
ISSN
0014-5793
DOI
10.1016/0014-5793(90)81531-r
language
English
LU publication?
no
id
03fec486-fec0-4bfc-8ad4-e2f8bdd2b83c
date added to LUP
2021-10-27 13:27:04
date last changed
2024-01-12 02:55:01
@article{03fec486-fec0-4bfc-8ad4-e2f8bdd2b83c,
  abstract     = {{<p>Three different carbohydrate prosthetic groups associated to three chymotryptic peptides, Q1, Q2 and Q3, were isolated from the reduced and carboxymethylated human protein HC. The first oligosaccharide forms an O-glycosidic linkage with a threonine residue at position 5 in the polypeptide chain of protein HC. The second and third carbohydrate prosthetic groups form N-linkages with asparagine residues at positions 17 and 96. Oligosaccharides present in Q1 contain 1 residue of NANA, 2 of GalNAc and 1 of Gal corresponding to the following structure: -O-GalNAc-GalNAc-Gal-NANA. Q2 contains 3 NANA, 9 GlcNAc, 2 Gal and 3 Man, and Q3 contains 2 NANA, 5 GlcNAc, 1 Gal and 2 Man. The sugar compositions of Q2 and Q3 oligosaccharides are compatible with that of the complex kind. The amount of oligosaccharides present in Q1, Q2 and Q3 corresponded respectively to 3.0%, 12.2% and 7.3% of the weight of protein HC. No difference was found between the carbohydrate composition of urinary and plasma protein HC.</p>}},
  author       = {{Escribano, J and Lopex-Otin, C and Hjerpe, A and Grubb, A and Mendez, E}},
  issn         = {{0014-5793}},
  keywords     = {{Alpha-Globulins/ultrastructure; Amino Acid Sequence; Amino Acids/analysis; Carbohydrates/analysis; Chromatography, High Pressure Liquid; Glycoproteins/ultrastructure; Humans; Molecular Sequence Data; Peptide Fragments/analysis}},
  language     = {{eng}},
  number       = {{1-2}},
  pages        = {{167--170}},
  publisher    = {{Wiley-Blackwell}},
  series       = {{FEBS Letters}},
  title        = {{Location and characterization of the three carbohydrate prosthetic groups of human protein HC}},
  url          = {{http://dx.doi.org/10.1016/0014-5793(90)81531-r}},
  doi          = {{10.1016/0014-5793(90)81531-r}},
  volume       = {{266}},
  year         = {{1990}},
}