Journal Details


Volume Number:  4
Jurnal Name:  Efflatounia

Authors: 
               Tahany H. Ayaad

Title:
ISOLATION, CHARACTERIZATION, AND N-TERMINAL AMINO ACID SEQUENCE OF LECTIN FROM PLASMA OF SCHISTOCERCA GREGARIA

Keywords: 
Lectin, hemagglutination activity, inhibition, isolation, amino acid sequence, Schistocerca gregaria .

Abstract:
A lectin with high hemagglutination activity was identified in the plasma of both male and female adult Schistocerca gregaria . The activity of the plasma lectin towards rabbit erythrocytes is efficiently inhibited by galactosides containing -16-linkage and by -m-, and -p-nitrophenyl-D-galactopyranosides. The lectin was isolated by affinity chromatography using -methyl-D-galactose-Sepharose 6B column, and eluted by 0.3 M raffinose solution in Tris buffer saline/Ca-Mg (TBS/Ca-Mg). Electrophoretic separation by reducing and non-reducing SDS-PAGE revealed that the lectins of both male and female are represented by one band with a molecular weight of ~ 80 KDa. The native lectin separated by non-denaturing PAGE lies in the high molecular weight range; indicating that it is formed of multiple subunits of ~ 80 KDa each. The lectin activity of both isolated and crude plasma forms are heat labile, and Ca-Mg dependent. The N-terminal amino acid sequence (60-amino acid residues) of the isolated lectin of Sc. gregaria revealed 63% identity with lectin precursor of the black locust Robinia pseudoacacia . Also, it has significant homology to some of the known vertebrate proteins sequenced to date; from which are the “human heparin-binding growth factor 1 receptor” with 100% identity, and the “insulin-like growth factor 1 receptor” with 42% identity.

Paper Pdf. File:
Paper Pdf. File
http://www.efflatounia.com/files/04-02.pdf