Jolivet P, Boulard C, Beaumal V, Chardot T, Anton M
Institut National de la Recherche Agronomique, Institut National Agronomique Paris-Grignon, UMR 206, Laboratoire de Chimie Biologique, Centre de Biotechnologie Agro-Industrielle, 78850 Thiverval-Grignon, France.
J Agric Food Chem. 2006 Jun 14;54(12):4424-9. doi: 10.1021/jf0531398.
To identify apoproteins present in purified low-density lipoproteins from hen egg yolk in relation with their emulsifying properties, they have been separated by SDS-PAGE. We identified two different proteins by liquid chromatography-tandem mass spectrometry analysis of the peptides obtained by the trypsin digestion of protein gel bands. Apovitellenin I was identified as a monomer and a dimer. Its amino acid sequence was totally confirmed, and molecular mass determination by liquid chromatography-mass spectrometry showed that it did not present post-translational modifications but only a slight heterogeneity by the loss of one or two amino acids at the C-terminal part of the protein. Apolipoprotein B was identified into seven bands corresponding to fragments resulting of a processing of the hen blood apo-B protein. The identity of the fragments was determined by the observation of the sequence coverage by trypsin peptides and the sequence alignment with homologous human blood apolipoprotein B-100.
