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, NURSEL and AYVALI, CEVAT (2002) "Purification and Determination of the Molecular Structure of Hemolymph Lectin of Agrotis segetum (Denis and Schiff.)," Turkish Journal of Biology: Vol. 26: No. 2, Article 1. Available at: https://journals.tubitak.gov.tr/biology/vol26/iss2/1
