Location and characterization of the three carbohydrate prosthetic groups of human protein HC
(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)
- author
- Escribano, J ; Lopex-Otin, C ; Hjerpe, A ; Grubb, A LU and Mendez, E
- publishing date
- 1990
- 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
-
- pmid:1694784
- scopus:0025344805
- 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}}, }