scholarly journals Serum proteins and the livetins of hen's-egg yolk

1962 ◽  
Vol 83 (2) ◽  
pp. 346-355 ◽  
Author(s):  
J WILLIAMS
Keyword(s):  
Serum Proteins ◽  
Egg Yolk ◽  
Hen’S Egg

STUDIES ON THE LIVETINS OF HEN'S EGG YOLK: II. IMMUNOELECTROPHORETIC IDENTIFICATION OF LIVETINS WITH SERUM PROTEINS

1964 ◽  
Vol 42 (8) ◽  
pp. 1119-1131 ◽  
Author(s):  
Chi-Ching Mok ◽  
R. H. Common
Keyword(s):  
Serum Albumin ◽  
Filter Paper ◽  
Laying Hens ◽  
Serum Proteins ◽  
Egg Yolk ◽  
Laying Hen ◽  
Immunoelectrophoretic Analysis ◽  
Hen’S Egg ◽  
Additional Antigen ◽  
Serum Antigens

Ten antigens have been distinguished in the sera of cocks and non-laying hens by immunoelectrophoretic analysis (IEA) against homologous rabbit antisera. An additional antigen has been found in the sera of laying hens by IEA against anti-laying-hen serum.Four of the serum antigens obtained by IEA have been correlated electrophoretically with the filter paper electrophoretic fractions serum albumin, serum α2-globulin, serum β-globulin, and serum γ-globulin.Serum albumin, serum α1-globulin, serum β-globulin, and serum γ-globulin have been identified immunologically with alpha-livetin, a livetin antigen (livetin 2), gamma1-livetin and gamma2-livetin respectively. Another antigen of cock serum and hen serum has been identified by IEA with a livetin antigen detected by IEA of livetin against anti-cock, anti-hen, and anti-yolk sera.

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.

Immunochemical analysis of the water-soluble fraction of the chick embryo yolk

Development ◽  
1970 ◽  
Vol 24 (1) ◽  
pp. 13-20
Author(s):  
C. E. Grossi ◽  
P. Carinci ◽  
L. Manzoli-Guidotti
Keyword(s):  
Serum Proteins ◽  
Soluble Fraction ◽  
Egg Yolk ◽  
Water Soluble ◽  
Immunochemical Analysis ◽  
Adult Chicken ◽  
Water Soluble Fraction ◽  
Chicken Serum ◽  
Protein Components ◽  
Immunochemical Techniques

By means of immunochemical techniques, the protein components of the water-soluble fraction (WSF) of the egg yolk have been examined in the unincubated egg and during incubation. Anti-ovalbumin and anti-total adult chicken serum antisera have been employed. Ovalbumin can be detected in the unincubated WSF as well as during incubation; its concentration seems to increase during incubation. In the WSF of the unincubated egg, six proteins immunologically related to adult serum proteins can be detected. They correspond to α-livetin, α1-globulin, β-livetin, ovotransferrin (conalbumin) and γ-livetin (two components). β-Livetin disappears after the 14th day of incubation while the other components can be demonstrated till hatching. The findings are discussed in relation to the data available in the literature. The findings are discussed in relation to the data available in the literature.

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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