• The Korean Journal of Zoology
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• v.35 no.4
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• pp.466-473
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• 1992

Storage protein-1 (SP-1) of Gallerio mellonella was identified in hemolvmph and fat body by electrophoresis. SP-1 was purified from hemolvmph by KBr density gradient ultracentrifugation , DEAE-cellulose (DE52) ion-exchange chromatography, and gel permeation chromatography (Sephadex G-200). Purity of SP-1 was confirmed by Non-SDS PAGE and electron microscope. SP-1 is 9.4 nm in diameter and regular octahedron in shape. SP-1 has isoelectric point of 5.7 and native molecular weight of 365 K dalton and is composed of one type of subunit with molecular weight of 82 K dalton. Ttiacylslvcerol and phospholipid were found to be maior lipid components in SP-1.

• The Korean Journal of Zoology
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• v.33 no.3
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• pp.346-353
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• 1990

Two storage proteins, storage protein-1 (SPl) and storage protein -2 (SP2) were found in hemolymph and fat body during the development of Lymantria dispar L. SP1 has a molecular weight of 440, 000 and consists of six identical subunits (MW = 72, 000). The pI value of SP1 was 6.2. SP1 shows a similar high concentration during the late larval stage in both male and female. However, SP1 represents a quite different pattern during pupal stage between male and female. SP1 gradually decreases in male but increases in female. SP1 is immunologically identical to yolk protein. Also, SP1 of L. dispar shows immunologically partial reactions with storage proteins of Hyphantria cunea and Galleria mellonella.