DISC GEL ELECTROPHORESIS OF PROTEINS IN NATIVE AND HEAT‐TREATED ALBUMEN, YOLK, AND CENTRIFUGED WHOLE EGG

SUMMARY– Polyacrylamide disc gel electrophoresis was an effective technique for resolving the proteins of albumen, yolk, and centrifuged whole egg into distinct bands. Albumen proteins including ovalbumins, conalbumins, and globulins were separated into 12 bands. Ovomucoid could not be detected and lysozyme did not migrate into the gel. With yolk, 19 bands including livetins and lipovitellins but not low-density lipoproteins were formed. When centrifuged whole egg was subjected to electrophoresis, livetin and albumen protein bands were detected, but no evidence was obtained for the formation of new protein complexes. Alterations of gel patterns were observed when albumen, yolk, and centrifuged whole egg were heated to pasteurization temperatures of 61.7°C and above.