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

FRACTIONATION AND DISSOCIATION OF THE AVIAN LIPOVITELLINS AND THEIR INTERACTION WITH PHOSVITIN

1964 ◽  
Vol 42 (3) ◽  
pp. 395-406 ◽  
Author(s):  
M. W. Radomski ◽  
W. H. Cook
Keyword(s):  
Ionic Strength ◽  
Phosphate Buffer ◽  
Structural Changes ◽  
Phosphorus Content ◽  
Egg Yolk ◽  
Gradient Elution ◽  
Progressive Change ◽  
Hen’S Egg ◽  
Dowex 1 ◽  
Elution Chromatography

Phosvitin and lipovitellin, the granule proteins of hen's egg yolk, were clearly separated by gradient elution on Dowex-1 columns. No phosvitin could be detected in the lipovitellin fraction but the first eluates of the phosvitin fraction contained lipovitellin of high protein phosphorus content. These initial eluates contained only two components sedimenting at rates slightly higher than dimer and monomer lipovitellin. As the lipovitellin monomer does not ordinarily occur in neutral solvents, the slower sedimenting material is either a new component or the monomer stabilized through interaction with phosvitin.Gradient elution chromatography of the total lipovitellins on hydroxyapatite showed that β-lipovitellin was completely eluted by 0.6 M phosphate buffer at pH 6.8 and appeared to be homogeneous. However, α-lipovitellin was heterogeneous: it was eluted over a concentration range of 0.7 to 1.4 M and the protein phosphorus content and dissociative behavior of successive fractions showed a progressive change with increasing ionic strength. Superimposed on this general heterogeneity of α-lipovitellin, there was consistent evidence of two poorly defined components, and three when the α-fraction was rechromatographed. Following dissociation and reassociation, there was no evidence of hybridization between monomers of α- and β-lipovitellin. Changes in the chromatographic patterns of α-lipovitellin following dissociation may indicate hybridization of different α-monomers, but these could also arise from structural changes in the monomers.

STUDIES ON THE LIVETINS OF HEN'S EGG YOLK: I. IDENTIFICATION OF PAPER-ELECTROPHORETIC AND IMMUNOELECTRO-PHORETIC LIVETIN FRACTIONS WITH SERUM PROTEIN ANTIGENS BY IMMUNOELECTROPHORETIC ANALYSIS

1964 ◽  
Vol 42 (6) ◽  
pp. 871-881 ◽  
Author(s):  
Chi-Ching Mok ◽  
R. H. Common
Keyword(s):  
Serum Protein ◽  
Egg Yolk ◽  
Paper Electrophoresis ◽  
Protein Antigens ◽  
Immunoelectrophoretic Analysis ◽  
Hen’S Egg ◽  
Alpha Beta

Immunoelectrophoretic analysis of an egg yolk livetin preparation has demonstrated the presence of six distinct fractions, which were numbered 1, 2, 3, 4, 5, and 6 from the anodic end of the electropherogram. Four of these fractions have been identified with four livetin fractions obtained by paper electrophoresis as follows: immunoelectrophoretic fraction 1 with alpha-livetin, fraction 2 with beta-livetin, fraction 4 with gamma1-livetin, and fraction 5 with gamma2-livetin.Immunoelectrophoresis of hen serum or cock serum against antilivetin serum has shown that both hen and cock sera contain antigens electrophoretically and immunologically identical to alpha-, beta-, gamma1-, and gamma2-livetins.

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