Molecular and immunological analysis of hen’s egg yolk allergens with a focus on YGP42 (Gal d 6)

2016 ◽  
Vol 71 ◽  
pp. 152-160 ◽  
Author(s):  
Chamika De Silva ◽  
Pathum Dhanapala ◽  
Tim Doran ◽  
Mimi L.K. Tang ◽  
Cenk Suphioglu
Keyword(s):  
Egg Yolk ◽  
Immunological Analysis ◽  
Hen’S Egg

6,8-Dihydroxypurine in the Hen’s Egg Yolk

1973 ◽  
Vol 28 (7-8) ◽  
pp. 482-483
Author(s):  
S. De Boeck ◽  
T. Rymen ◽  
J. Stockx
Keyword(s):  
Egg Yolk ◽  
Hen’S Egg

Characterization of glycopeptides derived from the low-density lipoprotein of hen's egg yolk

1968 ◽  
Vol 46 (8) ◽  
pp. 983-988 ◽  
Author(s):  
J. Z. Augustyniak ◽  
W. G. Martin
Keyword(s):  
Low Density Lipoprotein ◽  
Density Lipoprotein ◽  
Egg Yolk ◽  
Low Density ◽  
Amide Nitrogen ◽  
Acetylneuraminic Acid ◽  
Hen’S Egg ◽  
Terminal Amino ◽  
Protein Moiety

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.

The Osmotic Relations Between White and Yolk in the Hen's Egg

1932 ◽  
Vol 9 (3) ◽  
pp. 322-331
Author(s):  
J. B. BATEMAN
Keyword(s):  
Vapour Pressure ◽  
Freezing Point ◽  
Bound Water ◽  
Egg Yolk ◽  
Sodium Lactate ◽  
Point Of View ◽  
Protein Solutions ◽  
Hen’S Egg ◽  
Pressure Changes ◽  
Active Substances

1. The existence of a real osmotic difference between white and yolk of the hen's egg has been confirmed. 2. Hill's vapour-pressure thermopiles are shown to be reliable when used with viscous protein solutions such as egg-yolk. 3. The vapour-pressure changes which occur on mixing white and yolk indicate a removal of osmotically active substances. They do not agree with the freezing-point determinations of Straub. 4. The bearing of this result on the osmotic changes occurring in the fertilised and unfertilised egg is discussed. 5. The effects of diluting white and yolk with water and with various salt solution is studied from the point of view of 3 (above) and in relation to the problem of bound water. It is concluded that the amount of bound water in both white and yolk is small. The effect of solid sodium chloride on the vapour pressure of these substances confirms this conclusion. 6. Urea appears to dissolve in egg-white with normal depression of vapour pressure; urea and sodium lactate are largely removed from solution when added to yolk. Glucose is not so removed.

A simplified method for the purification of riboflavin-binding protein from hen's egg yolk

1979 ◽  
Vol 92 (2) ◽  
pp. 345-350 ◽  
Author(s):  
Usha S. Murthy ◽  
K. Sreekrishna ◽  
P.R. Adiga
Keyword(s):  
Binding Protein ◽  
Egg Yolk ◽  
Hen’S Egg ◽  
Simplified Method
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