scholarly journals Immunological Comparison of Native and Recombinant Hen’s Egg Yolk Allergen, Chicken Serum Albumin (Gal d 5), Produced in Kluveromyces lactis

Nutrients ◽  
2018 ◽  
Vol 10 (6) ◽  
pp. 757 ◽  
Author(s):  
Chamika De Silva ◽  
Pathum Dhanapala ◽  
Samuel King ◽  
Timothy Doran ◽  
Mimi Tang ◽  
...  
Keyword(s):  
Serum Albumin ◽  
Egg Yolk ◽  
Chicken Serum ◽  
Hen’S Egg ◽  
Immunological Comparison

STUDIES ON THE LIVETINS OF EGG YOLK: III. HETEROGENEITY AND IMMUNOELECTROPHORETIC BEHAVIOR OF BETA-LIVETIN

1966 ◽  
Vol 44 (10) ◽  
pp. 1357-1364 ◽  
Author(s):  
Shun-Fong Hui ◽  
R. H. Common
Keyword(s):  
Serum Albumin ◽  
Gel Electrophoresis ◽  
Egg Yolk ◽  
The Other ◽  
Positive Staining ◽  
Staining Reaction ◽  
Starch Gel Electrophoresis ◽  
Hen’S Egg ◽  
Starch Gel ◽  
The One

Starch-gel electrophoresis of the total livetins of hen's egg yolk resolved 16 zones: seven major zones, six minor zones, and three faint, diffuse zones. One zone was identified with the major component of paper electrophoretic alpha-livetin and hence with serum albumin. Four of the major zones were identified with the major components of paper electrophoretic beta-livetin on the one hand, and with an electrophoretically heterogeneous livetin antigen (livetin antigen 3) on the other hand, thus establishing the electrophoretic heterogeneity and relative immunological homogeneity of the paper electrophoretic beta-livetin fraction. The other two major starch-gel electrophoretic zones were identified as transferrins by their positive staining reaction for iron and comparison of their mobilities with two corresponding serum starch-gel fractions.

Egg yolk α-livetin (chicken serum albumin) is a cross-reactive allergen in the bird-egg syndrome

1994 ◽  
Vol 93 (5) ◽  
pp. 932-942 ◽  
Author(s):  
Z SZEPFALUSI ◽  
C EBNER ◽  
R PANDJAITAN ◽  
F ORLICEK ◽  
O SCHEINER ◽  
...  
Keyword(s):  
Serum Albumin ◽  
Egg Yolk ◽  
Chicken Serum

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.

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