Mutual solubility of the lipid components of egg yolk low-density lipoprotein

1968 ◽  
Vol 46 (8) ◽  
pp. 979-982 ◽  
Author(s):  
Henry Schneider ◽  
Neil H. Tattrie

Several aspects of the mutual solubility of the lipid components of the low-density lipoprotein of egg yolk have been investigated. The phospholipids were slightly soluble in the anhydrous triglycerides but became completely insoluble when water was present. Cholesterol showed a preference for the phospholipid phase both in the presence and absence of water. This partitioning behavior was taken to support the postulates that (i) the physicochemical properties of the lipids and their interactions with water may play a major role in controlling their spatial arrangement in the native lipoprotein, and (ii) the native lipoprotein contains a nucleus of almost pure triglyceride devoid of phospholipids which is surrounded by phospholipids and cholesterol.

1968 ◽  
Vol 46 (8) ◽  
pp. 983-988 ◽  
Author(s):  
J. Z. Augustyniak ◽  
W. G. Martin

Two glycopeptides (A and B) were isolated from pronase-digested vitellenin, the protein moiety of the low-density lipoprotein of hen's egg yolk. Aspartic acid was the only N-terminal amino acid of both glycopeptides but only A contained N-acetylneuraminic acid. A contained 55% hexose (mannose), 14% hexosamine, 12% N-acetylneuraminic acid, 0.71% amide nitrogen, and its molecular weight was 2.3 × 103. The corresponding values for B were 64, 17, 0.0, 0.75, and 2.0 × 103. Chemical analyses showed that B (and probably A) occurs in vitellenin with the heteropolysaccharide group bound N-glycosidically via the β-amide group of an asparaginyl residue. The indicated structure is R∙(NH)Asp∙Thr∙Ser∙(Ala, Gly, Val)∙Ile, where R, the heteropolysaccharide group, contains 2 hexosamine and 8 hexose residues.


2018 ◽  
Vol 97 (6) ◽  
pp. 2230-2238 ◽  
Author(s):  
N. Wang ◽  
Q. Xu ◽  
Y. Liu ◽  
Y. Jin ◽  
P.W. Harlina ◽  
...  

1963 ◽  
Vol 41 (2) ◽  
pp. 389-395 ◽  
Author(s):  
R. W. Burley

The absorption of chloroform by α- and β-lipovitellin from chloroform-saturated aqueous buffer solutions has been measured quantitatively. Absorption is rapid and reaches equilibrium values of 13 and 22% of the dry weights of α- and β-lipovitellin respectively. Ultracentrifugal examination of these lipovitellin solutions shows that chloroform absorption produces a heavier fraction that is not homogeneous and probably consists of aggregates. There appears to be a threshold concentration of chloroform in the aqueous solutions below which none is absorbed by the lipovitellins. Similar, but less extensive, experiments with the low-density lipoprotein of yolk and yolk lecithin have shown that they also absorb chloroform under the same conditions.


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