New insights into the structure of apolipoprotein B from low-density lipoproteins and identification of a novel YGP-like protein in hen egg yolk

被引:27
|
作者
Jolivet, Pascale [1 ,2 ]
Boulard, Celine [1 ,2 ]
Chardot, Thierry [1 ,2 ]
Anton, Marc [3 ]
机构
[1] INRA, F-78850 Thiverval Grignon, France
[2] AgroParisTech, UMR Chim Biol 206, F-78850 Thiverval Grignon, France
[3] INRA, UR Biopolymeres Interact Assemblages 1268, F-44316 Nantes, France
关键词
hen egg yolk; low-density lipoproteins; plasma proteins; LC-MS identification; structural proteomic strategy; enzymatic deglycosylation; proteinase K;
D O I
10.1021/jf800321m
中图分类号
S [农业科学];
学科分类号
09 ;
摘要
Apoproteins of low-density lipoproteins (LDL) and soluble proteins (livetins) contained in hen egg yolk plasma have been demonstrated as being essential to the interfacial and emulsifying properties of yolk. The knowledge of their structure is necessary to better understand these properties. Purified protein fractions were separated by SDS-PAGE or 2D-PAGE and identified through the LC-MS/MS of their trypsin peptides. Hen blood apolipoprotein B gives rise to nine different apoproteins in LDL after maturation and proteolysis. Among these apoproteins, two protein fragments appeared to be less accessible to proteases and could be enriched in beta-sheets and firmly associated with lipids. Plasma soluble proteins were constituted by similar to 45% of yolk immunoglobulins with a high heterogeneity of the variable regions of both heavy and light chains, 41% of glycoproteins constituted by YGP42 and YGP40, 14% of albumins, and one new minor protein we called YGP30, showing 75% similarity to YGP40.
引用
收藏
页码:5871 / 5879
页数:9
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