CHARACTERIZATION OF STORAGE PROTEIN, ARYLOPHORIN FROM THE HEMOLYMPHOF THE PEST, HELICOVERPA ARMIGERA

Abstract

Storage proteins, such as arylophorin, are synthesized from the fat body of a wide range of lepidopteran and dipteran larvae and also in other insect orders. Storage protein from hemolymph of H. armigera was obtained by ammonium sulphate fractionation and anion-exchange chromatography. From 1,500 mg of total protein, 7.35 mg of purified protein was acquired with 24.4% recovery. Subunit molecular weight of purified storage protein was estimated to be 66 kDa. The native molecular weight of the protein was determined to be 400 kDa. Amino acid composition showed that the protein was characterized by the presence of aromatic amino acids. Multiple amino acid sequence alignment of obtained LCMS sequence of the purified protein of H. armigera indicated that the protein is arylophorin. The deduced amino acid sequence was found to more homology with the arylphorins of Spodoptera litura, Manduca sexta, Hyalophora cecropia and Antherae apernyi.