Isolation and characterization of chicken thymic electrolectin

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Abstract
The presence of a .beta.-D-galactoside-binding lectin (electrolectin) was detected in extracts of the thymus of adult chickens. This lectin was purified by affinity chromatography on a lactosyl-Sepharose column to yield 1.4 mg of pure protein from 230g of thymus. The chicken thymic electrolectin (CTE) has MW of 15,300 when analyzed by sodium dodecyl sulfate/polyacrylamide gel electrophoresis and of 30,000 when analyzed by gel filtration. The amino acid composition of CTE is similar to that of other electrolectins purified from human and rat lung. CTE crossreacts immunologically, but is not identical, with electrolectins from electric-eel electric organ and from chick-embryo pectoral muscle. CTE agglutinates chicken thymocytes but does not appear to promote their mitosis.