Abstract
Summary
Ovotransferrin was prepared from duck (Anas platyrhynochos) egg white by ammonium sulfate precipitation and further purified by DEAE and CM sephadex chromatography in a final yield of 2.25 mg/ml egg white, forming about 2% of total solids of egg white. Duck ovotransferrin (DOT) was shown by starch gel electrophoresis to be comprised of a minor component with fast anodic mobility at pH 8.6 and a major component with slow mobility. Isoelectric focusing on sucrose gradient column revealed isoelectric points of the minor and major components as 5.52 ± 0.02 and 5.70 ± 0.02 pH units, respectively. These components gave identical reactions with a rabbit anti-DOT anti-serum by Ouchterlony double diffusion analysis. Anti-DOT antiserum agglutinated and lysed tanned sheep erythrocytes coated with minor component 25%-50% less than the erythrocytes similarly coated with the major component. Similar difference was also observed by the quantitative immuno-precipitation reaction of transferrin components with anti-DOT antiserum.
Dr. J. Williams, Molecular Enzymology Laboratories, Department of Biochemistry, University of Bristol Medical School, Bristol, England, is thanked for inducing the author's interest in the study of transferrins and for many helpful suggestions. Part of the chemical work was done by the author in the Bristol laboratory. The author is thankful to Dr. S. Das for assistance in hemagglutination assay and to Dr. W. Bard-awill, Director, Pathology and Medical Research, St. Margaret's Hospital, Boston, Massachusetts, for his interest and encouragement.
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