Chicken Serum Proteins: A Comparison of Electrophoretic Techniques and Localization of Transferrin

Abstract

INTRODUCTION ELECTROPHORETIC studies on chicken serum have been reported using various techniques. Five distinct peaks were observed by moving-boundary electrophoresis (Moore, 1948); 5–6 bands were demonstrated by paper electrophoresis (Common and McKinley, 1953; McKinley et al., 1953); and 6–7 bands were identified using cellulose acetate electrophoresis (Longenecker et al., 1967; Beg and Clarkson, 1970). Incorporating the molecular sieving concept, 12–15 bands were found by starch-gel electrophoresis (Amin, 1961; Ogden et al., 1962); and from 10 to 19 bands were distinguished using polyacrylamide-gel electrophoresis (Glick, 1968; Harris and Sweeney, 1969). Transferrin, the iron-binding protein in serum, has been studied in chickens by the moving-boundary method (Marshall and Deutsch, 1951), by starch-gel technique (Ogden et al., 1962; Williams, 1962), and by polyacrylamide-gel electrophoresis (Glick, 1968; Prosky et al., 1968). However, location of transferrin in the electrophoretic pattern of chicken serum performed on paper or cellulose acetate has not been…