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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
Author(s) -
Parkinson T. L.
Publication year - 1972
Publication title -
journal of the science of food and agriculture
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.782
H-Index - 142
eISSN - 1097-0010
pISSN - 0022-5142
DOI - 10.1002/jsfa.2740230516
Subject(s) - ovalbumin , egg white , yolk , electrophoresis , chemistry , egg albumen , ovotransferrin , chromatography , biology , electropherogram , biochemistry , food science , immunology , antigen
Zone electrophoresis assisted in the identification of several of the fractions isolated from white, yolk and whole egg, and particularly in following the distribution of the ovalbumin homologues. Certain artifacts in electropherograms of ovalbumin fractions were attributed to aggregation of this substance during freeze‐drying. The ovalbumin in whole egg appears to have a slightly higher affinity for diethylaminoethylcellulose than when it is present in egg white only. Characteristics of some unidentified proteins are noted. The implications of all the findings are discussed and the susceptibility of the low density fraction of egg yolk to environmental change is emphasised.