Separation of the proteins of egg white and egg yolk and a study of their interactions in whole egg. IV. Electrophoretic studies

Parkinson, T. L.

doi:10.1002/jsfa.2740230516

Cited by 8 publications

(3 citation statements)

References 12 publications

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“…They nevertheless failed to discriminate all egg white proteins. Promising complementary separation methods include electrophoretic separations, which recently underwent considerable improvements, whereas the last studies on egg white proteins, in this field, date from the 1960s and 1970s ( − ). SDS−PAGE followed by Coomassie blue detection is the only technique described in recent work for the study of egg white proteins ( , ).…”

Section: Introductionmentioning

confidence: 99%

Comparison of Different Electrophoretic Separations of Hen Egg White Proteins

Désert¹,

Guérin-Dubiard²,

Nau³

et al. 2001

J. Agric. Food Chem.

104

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The hen egg white protein composition has not yet been fully defined. To improve the knowledge of this biological fluid, the most usual and recently developed electrophoretic methods have been used: SDS-PAGE, native-PAGE, isoelectric focusing (IEF), and 2-dimensional electrophoresis (2DE). Seven of the major known proteins were thus identified in at least one electrophoretic system. Isoforms of ovotransferrin, ovalbumin, and ovomucoid were visualized when pI was used for the separation. Two-dimensional electrophoresis allowed separation of a very large number of spots. In each of the four systems, some components were revealed but not identified, and unknown spots were particularly numerous with 2DE. With this technique, many spots corresponding to small acidic proteins were highlighted, among which was the Ch21 protein, whose presence in hen egg white was thus confirmed. This study thus constitutes, to our knowledge, the first proteomic investigation of hen egg white.

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Section: Introductionmentioning

confidence: 99%

Comparison of Different Electrophoretic Separations of Hen Egg White Proteins

Désert¹,

Guérin-Dubiard²,

Nau³

et al. 2001

J. Agric. Food Chem.

104

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“…Electrophoresis on cellulose acetate strips and in polyacrylamide gels was carried out as described previously. 5 Electrophoresis on paper strips (Whatman No. 1) was conducted according to Powrie et al6 After electrophoresis the strips were cut in half lengthwise, one half was stained with bromophenol blue (for proteins) and the other with Oil Red 0 (for lipids).…”

Section: Electrophoresismentioning

confidence: 99%

Effects of spray‐drying and freezing on the proteins of liquid whole egg

Parkinson¹

1975

J Sci Food Agric

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Commercial pasteurised liquid whole egg was spray-dried, both alone and mixed with liquid milk, and some of it was frozen. Paper electrophoresis revealed that lipoprotein fractions from the pasteurised liquid egg were mainly immobile, in contrast to unpasteurised new-laid egg which contained both mobile and immobile lipoprotein fractions. The major difference between the soluble proteins of the commercial chilled pasteurised liquid egg and those of the same egg after freezing and thawing was the presence, in the former, of an inert lipoprotein fraction, amounting to 3.6% of the total egg solids and containing 88% lipid. The "soluble" proteins of spray-dried egg and egg-milk mixture also included large "inert" lipoprotein fractions eluted with the void volume.They contained 72-81 % of lipid and accounted for 7-13 % of the total egg solids. Larger fractions were eluted by the stronger salt buffer solutions and by hydrochloric acid from the dried egg-milk mixture than from the dried egg, and these were probably derived from the milk. All the spray-dried samples possessed the "inert insoluble" protein fraction characteristic of liquid egg, and the presence of a high molecular weight lipoprotein fraction was confirmed in each case. The "insoluble proteins" of the spray-dried samples had higher protein contents than those from the original chilled liquid egg and the thawed frozen egg.

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“…More recently, disc-gel electrophoretic separations of chicken egg yolk have been reported (Silano et al 1968;Chang et al 1970;Harduf and Alumot 1971;Parkinson 1972;Cummingham and Varadarajulu 1973;Shantz and Dawson 1974). Seideman and Cotkrill (1969) reported spe ies differences in the cation-exchange chromatograms of chicken, turkey, and goose egg yolk.…”

Section: Introductionmentioning

confidence: 99%

A Study of Turkey Egg Yolk 1. Composition and Electrophoretic Separation of Components

Cunningham

Lee

1978

J Food Biochemistry

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Yolks from fresh eggs produced by Broad Breasted White turkeys were blended and analyzed. Proximate composition was determined and components were separated in 7% polyacrylamide gel. Turkey egg yolk was compared with chicken egg yolk. Turkey egg yolk contained a higher percentage of solids, fat, and protein than chicken egg yolk. When separated electrophoretically, components of chicken egg yolk migrated faster than those in turkey egg yolk. Turkey yolks could be resolved into 10 or 11 distinct components; chicken yolk, into 11 or 12 components, depending on electrophoretic technique.

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Separation of the proteins of egg white and egg yolk and a study of their interactions in whole egg. IV. Electrophoretic studies

Cited by 8 publications

References 12 publications

Comparison of Different Electrophoretic Separations of Hen Egg White Proteins

Comparison of Different Electrophoretic Separations of Hen Egg White Proteins

Effects of spray‐drying and freezing on the proteins of liquid whole egg

A Study of Turkey Egg Yolk 1. Composition and Electrophoretic Separation of Components

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