scholarly journals Egg Quality from Avian Species: Electrophoretic Characterization of Egg White Proteins

2021 ◽  
pp. 34-43
Author(s):  
Meziani Samira ◽  
Drici Amine El-Mokhtar ◽  
Menadi Noureddine ◽  
Diaf Mustapha ◽  
Zairi Mohammed ◽  
...  
Keyword(s):  
Gel Electrophoresis ◽  
Quantitative Difference ◽  
Qualitative Difference ◽  
Bird Species ◽  
Egg Yolk ◽  
Egg White ◽  
Agarose Gel ◽  
Agarose Gel Electrophoresis ◽  
Egg White Proteins

The aim of the present study was to evaluate and to compare the physicochemical composition of egg white, and to characterize and estimate the quantitative variations of egg white proteins of different birds’ species (duck, quail, Chicken, partridge and goose). For each bird species, the whole egg temperature, weight, height, density and shape index were evaluated. After breaking the eggs, a visual examination was performed then vitelline (VI) and albumen (AI) indexes and the haugh unit (HU) were measured. The study of the quality and the characterization of egg white proteins were performed by Agarose Gel Electrophoresis. The total egg weight varied within a range of (8.98±0.82 g to 142.91±10.34 g) for quail and goose, respectively. The thickness of the egg yolk was almost three times higher than that of the egg white in all breeds. The egg freshness, measured by HU, was higher in partridge, followed by quail and chicken breeds with values of 88.81±0.09, 87.45±3.33, 81.53±2.16, respectively. The VI shows values of about 0.40. The egg yolk/ white ratio ranged from 47 and the pH varied from 8.37 to 8.95 for all local species studied. The egg white protein content was higher for all species (up to 14.45g/100 g). Three types of proteins are identified by agarose gel electrophoresis (ovalhibitor, ovotransferrin and ovalbumin) with a quantitative difference between bird species. Densitometric analysis shows a qualitative difference due to the presence of type C lysozyme in chicken egg white.

scholarly journals Variation of egg proteins between bird varieties by using SDS-PAGE

2019 ◽  
Vol 12 (1) ◽  
pp. 68-73
Author(s):  
Questan Amin ◽  
Hemn Zhahir ◽  
Ahmed Shaker
Keyword(s):  
Sodium Dodecyl Sulfate ◽  
Trypsin Inhibitor ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Egg Yolk ◽  
Egg White ◽  
Yolk Proteins ◽  
Egg White Proteins ◽  
Sds Page

Proteins are essential constituents of all organisms; both egg white proteins and egg yolk are source of protein. The aim of this study was conducted to perform preliminary studies to analyses and compare egg white proteins and yolk proteins from different avian species (guineafowl, dwarf hens, local hen, Shami, turkey, duck, geese, partridge and quail) via or with SDS-PAGE (Sodium Dodecyl Sulfate–Polyacrylamide Gel Electrophoresis ). 18 Fresh eggs of different poultry species (guineafowl, dwarf hens, local hen, Shami, turkey, duck, geese, partridge and quail) were collected from various farms in the Sulaimani province. Data on egg proteins were analyzed using Statistical Xlstate used for dendrogram construction and PCA. The main egg white proteins were Ovomicin, Ovotransferrin, Ovalbumin, Flavoprotein, α- chymotrypsinogen, and Trypsin inhibitor. The main lipoproteins were Apovitellenin VI, Apovitellenin Vb, Apovitellenin V, Apovitellenin IIIa, Apovitellenin III, Apovitellin 7, B-Livetin, Apovitellenin IIa, Apovitellenin II, and Apovitellenin I. All these lipoproteins were observed in the nine birds species. The egg white proteins and yolk lipoproteins for nine species were examined. It can be concluded the large differences were found in a mount of egg white proteins and yolk lipoproteins of the nine species of birds.

scholarly journals Performance Comparison of Capillary and Agarose Gel Electrophoresis for the Identification and Characterization of Monoclonal Immunoglobulins

2008 ◽  
Vol 129 (3) ◽  
pp. 451-458 ◽  
Author(s):  
Christopher R. McCudden ◽  
Stephanie P. Mathews ◽  
Shirley A. Hainsworth ◽  
John F. Chapman ◽  
Catherine A. Hammett-Stabler ◽  
...  
Keyword(s):  
Gel Electrophoresis ◽  
Performance Comparison ◽  
Agarose Gel ◽  
Agarose Gel Electrophoresis ◽  
Monoclonal Immunoglobulins ◽  
Identification And Characterization

Characterization of eight VNTR loci by agarose gel electrophoresis

Genomics ◽  
1989 ◽  
Vol 5 (4) ◽  
pp. 915-924 ◽  
Author(s):  
S.J. Odelberg ◽  
R. Plaetke ◽  
J.R. Eldridge ◽  
L. Ballard ◽  
P. O'Connell ◽  
...  
Keyword(s):  
Gel Electrophoresis ◽  
Agarose Gel ◽  
Agarose Gel Electrophoresis

Rapid detection and characterization of plant virused by agarose gel electrophoresis: Size, surface charge and heterogeneity of panicum mosaic and related viruses

1984 ◽  
Vol 5 (4) ◽  
pp. 202-208 ◽  
Author(s):  
Philip Serwer ◽  
Elena T. Moreno ◽  
Shirley J. Hayes ◽  
Philip Berger ◽  
Marie Langham ◽  
...  
Keyword(s):  
Surface Charge ◽  
Gel Electrophoresis ◽  
Rapid Detection ◽  
Agarose Gel ◽  
Agarose Gel Electrophoresis

Characterization of Recombinant von Willebrand Factors Mutated on Cysteine 509 or 695

1996 ◽  
Vol 76 (03) ◽  
pp. 453-459 ◽  
Author(s):  
Virginie Siguret ◽  
Anne-Sophie Ribba ◽  
Olivier Christophe ◽  
Ghislaine Chérel ◽  
Bernadette Obert ◽  
...  
Keyword(s):  
Gel Electrophoresis ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis ◽  
Agarose Gel ◽  
Agarose Gel Electrophoresis ◽  
Mutant Proteins ◽  
Von Willebrand ◽  
High Molecular Weight Multimers

SummaryThe interacting domain of vWF with platelet GPIb has been shown to overlap the large A1 loop formed by the intra-chain disulfide bond linking Cys 509 to Cys 695. In order to further investigate the role of the conformation of this region, we have expressed in COS-7 cells three mutated full-length recombinant vWFs (rvWFs) in which the substitutions Cys509Gly, Cys509Arg or Cys695Gly have been introduced by site-directed mutagenesis. SDS-agarose gel electrophoresis demonstrated an impaired multimerization of the mutants with undetectable high molecular weight multimers and a decrease of the relative amounts of the intermediate sized multimers. Binding analysis showed that rvWFC509G and rvWFC509R did not interact with botrocetin but spontaneously interacted with GPIb; the latter binding remained unchanged in the presence of ristocetin. This indicates that the substitution of Cys509 by Gly or Arg creates a conformation of vWF that increases its binding to GPIb. In contrast, rvWFC695G which did not react with botrocetin was also unable to interact with GPIb even in the presence of ristocetin, indicating that sequences interacting with GPIb are masked and/or disrupted. In conclusion, the substitution of each of the Cys509 and 695 results in mutant proteins which may be “locked” into active or inactive conformations in regard to the binding to platelet GPIb receptor.

Applicability of agarose gel electrophoresis to the physical characterization of clathrin-coated vesicles

1985 ◽  
Vol 147 (2) ◽  
pp. 353-363 ◽  
Author(s):  
Melvin H. Gottlieb ◽  
Clifford J. Steer ◽  
Alasdair C. Steven ◽  
Andreas Chrambach
Keyword(s):  
Gel Electrophoresis ◽  
Coated Vesicles ◽  
Physical Characterization ◽  
Agarose Gel ◽  
Agarose Gel Electrophoresis
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