JDS
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

Journal of Dairy Science Vol. 77 No. 5 1205-1215
© 1994 by American Dairy Science Association ®
This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Girardet, J.-M.
Right arrow Articles by Spik, G.
Right arrow Search for Related Content
PubMed
Right arrow Articles by Girardet, J.-M.
Right arrow Articles by Spik, G.

High Performance Electrophoresis Chromatography of Bovine Milk Component 3 Glycoproteins

Jean-Michel Girardet 1, Franck Saulnier 1, Alain Driou 1, Guy Linden 1, Bernadette Coddeville 2, and Genevieve Spik 2

1 Laboratoire de Biochimie Appliquée, Associé à l'Institut National de Recherche Agronomique, Université de Nancy, BP 239, 54506 Vandoeuvre les Nancy Cedex, France
2 Laboratoire de Chimie Biologique, Unité Mixte de Recherche du Centre National de la Recherche Scientifique No. 111, Université des Sciences et Technologies de Lille, 59655 Villeneuve d'Ascq Cedex, France

Component 3 corresponds to the hydrophobic fraction of bovine milk proteose-peptone and is composed of three principal glycoproteins with molecular masses of 11, 19, and 29 kDa. To understand better its interesting emulsifying properties and its capability of inhibiting spontaneous lipolysis in milk, isolation and characterization of the three glycoproteins are needed. The newly introduced technique of high performance electrophoresis chromatography is an efficient tool to prepare these glycoproteins in high purity. This preparative technique offers the resolving power of gel electrophoresis with the automatization associated with HPLC. Parameters that influence protein separation are discussed. The isolated 19- and 29-kDa glycoproteins, which bind to immobilized concanavalin A, are then characterized by analysis of their glycan and amino acid compositions. In particular, the glycan molar ratio of the 19-kDa glycoprotein is in good agreement with a biantennary N-acetyllactosamine-type glycan structure.

Key Words: high performance electrophoresis chromatography • proteose-peptone • milk • glycoprotein

Submitted on January 11, 1993
Accepted on November 19, 1993






HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 1994 by the American Dairy Science Association ®.