Turkish Journal of Biology
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.
DOI
-
Keywords
Agrotis segetum, lectin (agglutinin), purification, molecular weight, transmission electron microscopy (TEM)
First Page
49
Last Page
55
Recommended Citation
GÜL, N, & AYVALI, C (2002). Purification and Determination of the Molecular Structure of Hemolymph Lectin of Agrotis segetum (Denis and Schiff.). Turkish Journal of Biology 26 (2): 49-55. https://doi.org/-
