미국흰불나방(H. cunea)의 저장단백질-1(Storage Protein-1; SD-1)을 종령유충의 혈림프에서 확인하고, KBr 농도구배 초원심분리의 방법으로 정제하였댜. 정제된 SP-1의 순수도는 전기영동법으로 확인하였다. SP-1의 분자량은 460kD이었으며 76.7kD의 한 종류 구성소단위로 구성되어 있다. SP-1을 thin layer chromatography로 지질 분석한 결과 1.2-와 1,3-diglyceride로 구성되어 있었으며, 지방산은 주로 lauric acid와 palmitoleic acid로써 이루어져 있었다. 또한, SP-1을 구성하고 있는 아미노산 중에는 valine이 많은 양을 차지하고 있었다. 지방체와 난소내에 SP-1의 존재는 SP-1에 대한 항체를 이용한 Western blotting 방법으로 확인하였으며, 난소의 단백질체에 축척된 SP-1은 immunogold labelling방법을 이용하여 전자현미경으로써 관찰하였다.
Storage protein-1 (SP-1) of Hyphantria cunea Drury was confirmed from hemolymph of last instar larva and purified using KBr density gradient ultracentrifugation, ion exchange chromatography and gel permeation chromatography. The purity of isolated SP-1 was demonstrated by polyacrylamide gel electrophoresis. The native molecuar weight of SP-1 was determined to be 460kD by gel permeation chromatography. The SP-1 was hexamer that consisted of single type subunit (76.7kD). The lipids in SP-1 were detected by thin layer chromatography and comprised 1, 2- and 1, 3-diglyceride. The fatty acids in lipids were confirmed to be lauric acid and palmitoleic acid. Amino acid analysis showed that valine was predominant among amino acids in SP-1. The presence of SP-1 in the fat body and ovary was found by western blotting using SP-1 antiserum. Electron microscopy of immunogoldlabeled ovarian tissue indicated that SP-1 accumulated in protein bodies of the ovary.
