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Turkish Journal of Biology

DOI

-

Abstract

A soluble lectin was purified from the hemolymph of Agrotis segetum by two methods, via affinity chromatography on a Sepharose-4B column and gel filtration on a Superdex-200 column. Sodium Dodecyl Sulfate-Polyacrylamide Gel Electrophoresis (SDS-PAGE) showed a single protein band with a molecular weight of 69,000 in both the presence and absence of 2-Mercaptoethanol. Alternatively, the molecular weight of this lectin was estimated to be 69,000 by gel filtration on Superdex-200. Electron microscopic observation of the purified lectin was reticular in structure and consisted of tandem aligned spherical basic units.

First Page

49

Last Page

55

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