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PMID: 3149515 Published · ppublish English Comparative Study Journal Article Research Support, Non-U.S. Gov't

Comparative study of the primary structures of sero-, lacto- and ovotransferrin glycans from different species.

Biochimie ·Vol. 70 ·No. 11 ·1988-11-00 ·Pages 1459-69

Spik G, Coddeville B, Montreuil J

Abstract

In order to establish relationships between glycan structure and biological activity and to answer the question: Are glycans markers of evolution?, the authors undertook a comparative study of the glycan primary structures of different transferrins (sero-, lacto- and ovotransferrins) from several species. By associating permethylation--mass spectrometry and 1H NMR spectroscopy, the primary structure of the following transferrin glycans were determined: human, bovine, hen, horse, marsupial, mouse, rabbit, rat and sheep serotransferrins; human, mouse, bovine and goat lactotransferrins; hen and turkey ovotransferrins. The results obtained led to the conclusion that transferrin glycans are specific for each transferrin and, for a given transferrin, specific to the species. No relationship could be established a priori between primary structure and function of transferrin glycans.

MeSH Terms
Animals Biological Evolution Carbohydrate Conformation Carbohydrate Sequence Conalbumin Female Humans Lactoferrin Molecular Sequence Data Molecular Structure Polysaccharides Species Specificity Structure-Activity Relationship Transferrin
Chemicals
Polysaccharides Transferrin Conalbumin Lactoferrin
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Spik G
Université des Sciences et Techniques de Lille Flandres-Artois, Laboratoire de Chimie Biologique (Unité Associée au CNRS No. 217), Villeneuve-d'Ascq, France.
Coddeville B
Montreuil J
Article Info
Journal
Biochimie
Abbr.
Biochimie
ISSN
0300-9084
Published
1988-11-00
Pages
1459-69
Language
English
Region
France
NLM ID
1264604
Subset
IM
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