Comparative analysis of storage proteins of fall webworm (Hyphantria cunea, Drury)

Comparative Biochemistry and Physiology. Part B, Biochemistry & Molecular Biology
J K SongH R Kim

Abstract

Two kinds of storage protein (SP-1 and SP-2) were purified from the hemolymph of last instar larvae of Hyphantria cunea by ultracentrifugation, chromatofocusing, and ion-exchange chromatography. SP-1 and SP-2 each consist of six subunits and have the molecular mass of 79 KDa and 82.5 KDa, respectively. These showed different patterns of appearance in fat body and hemolymph, and different SDS-PAGE patterns in non-reducing gels. Their stability in citrate-phosphate or Tris-HCl buffers differs and their immunological characteristics indicates that these are different storage proteins. Comparison with storage proteins of other species with respect to amino acid composition and N-terminal sequence, indicates that SP-1 can be classified as a methionine-rich storage protein but SP-2 cannot be regarded as a classical arylphorin.

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Citations

Jul 19, 2002·Archives of Insect Biochemistry and Physiology·Hyang-Mi CheonSook-Jae Seo
Oct 24, 2001·Archives of Insect Biochemistry and Physiology·H M CheonS J Seo
May 29, 2003·Journal of Insect Physiology·N P. GudderraR M. Roe
Jan 16, 2002·Comparative Biochemistry and Physiology. Toxicology & Pharmacology : CBP·C S ChoiH R Kim
May 5, 2001·Comparative Biochemistry and Physiology. Part B, Biochemistry & Molecular Biology·S J HwangS J Seo
Mar 23, 2006·Archives of Insect Biochemistry and Physiology·Chi Won ChoiChi-Young Yun
May 30, 2009·Archives of Insect Biochemistry and Physiology·Yijia LiGuoping Huang

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