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Article Dans Une Revue Journal of Agricultural and Food Chemistry Année : 2006

Protein components of low-density lipoproteins purified from hen egg yolk

Résumé

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.

Dates et versions

hal-02665302 , version 1 (31-05-2020)

Identifiants

Citer

Pascale P. Jolivet, Celine C. Boulard, Valerie Beaumal, Thierry T. Chardot, Marc Anton. Protein components of low-density lipoproteins purified from hen egg yolk. Journal of Agricultural and Food Chemistry, 2006, 54 (12), pp.4424-4429. ⟨10.1021/jf0531398⟩. ⟨hal-02665302⟩
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