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

Biochimie. 1988 Nov;70(11):1459-69. doi: 10.1016/0300-9084(88)90283-0.

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.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

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*

Substances

  • Polysaccharides
  • Transferrin
  • Conalbumin
  • Lactoferrin