• The Korean Journal of Zoology
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• v.37 no.4
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• pp.488-494
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• 1994

Apolipophorin-III (ApoLp-III) was purified from adult haemolynph of Hyphantriu cuneo and their molecular weight and synthetic place were investigated. ApoLp-III purification was performed by KBr-density gradient ultracentrifugation followed by gel permeation chromatographv (Sephadex G-1001 and ion-exchange chromatography (CM-52) and their purity was confirmed on 10% SDS-PAGE. ApoLp-III has the molecular weight of 18 ItDa and is synthesized by fat body.

• International Journal of Industrial Entomology and Biomaterials
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• v.3 no.2
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• pp.163-168
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• 2001

We isolated and sequenced a cDNA clone corresponding to apolipophorin-III (apoLp-III) from the fall webworm, Hyphantria cunea. The cDNA for apoLp-III codes fer a 187-residue protein (561 bp) with a predicted molecular mass of 20 kDa. The calculated isoelectric point is 8.76. Multiple alignment analysis of the amino acid sequence revealed that H. cunea apoLp-III is most similar to that of Spodoptera litura (71.5% identity), followed by that of Manduca sexta (69.7% identity). They share five amphipathic $\alpha$-helices that are proposed to play a critical role in the binding of apoLp-III to lipophorin.

• Journal of the Korea Academia-Industrial cooperation Society
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• v.14 no.8
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• pp.4106-4110
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• 2013

Apolipophorin-III (apoLp-III) was isolated and purified from the last larval hemolymph of Galleria mellonella by the KBr gradient ultracentrifugation and gel chromatography (Sephadex G-100). In this paper, we examined that apoLp-III is taken up into the last larval fat bodies in Galleria mellonella. The last larval fat body tissues were incubated at room temperature for 30 min with fluorescein isothiocyanate (FITC)-labeled apoLp-III (FITC-apoLp-III). Fluorescein microscopy and sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis (PAGE) revealed that the last larval fat body tissues internalize FITC-apoLp-III. The results show that the apoLp-III is taken up by the last larval fat body.

• Journal of the Korea Academia-Industrial cooperation Society
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• v.10 no.3
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• pp.620-624
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• 2009

Apolipophorin-III (apoLp-III) was isolated and purified from the last instar larval hemolymph of Galleria mellonella by gel chromatography (Sephadex G-100) and ion exchange chromatography (CM-52). In the present study, I wanted to show that apoLp-III is taken up into the adult ovary in Galleria mellonella. Adult ovary tissues were incubated at room temperature for 30 min with fluorescein isothiocyanate (FITC)-labeled apoLp-III. Fluorescence microscopy and sodium dodecylsulfate (SDS)-polyacrylamide gel electrophoresis (PAGE) revealed that adult ovary tissues internalize fluorescence-labeled apoLp-III. The results suggest that apoLp-III is taken up by the adult ovary.

• International Journal of Industrial Entomology and Biomaterials
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• v.7 no.2
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• pp.145-149
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• 2003

ApolipophorinIII (apoLp-III) is a protypical exchangeable apolipoprotein that is abundant in hemolymph of many insect species. Its function lies in the stabilization of low-density lipophorin particles (LDLp) crossing the hemocoel in phases of high energy consumption to deliver lipids from the fat body to the flight muscle cells. But, recent studies with naive Galleria mellonella-apoLp-III gave first indication of an unexpected role of that protein in insect immune activation. In this research, we cloned a cDNA encoding putative apoLp-III from the silkworm, Bombyx mori injected with E. coli and characterized its role. We constructed a cDNA library using whole bodies of B. mori larvae injected with E. coli, carried out the differential screening, and selected the up-regulated clones. Among these clones, we focused on a cDNA showing a high sequence similarity to the apolipophorinIII from other insects and analyzed the nucleotide and deduced amino acid sequences. The pupative B. mori Jam123 apoLp-III cDNA contained 1,131 bp encoding 186 amino acid residues. Phylogenetic analysis revealed that the nucleotide and amino acid sequences of the B. mori apoLp-III cDNA formed a highly inclusive subgroup with Bombycidae. But, it was interesting that B. mori Jam123 is closer to B. mandarina than B. mori P50 and B. mori N4. Northern blot analysis showed a signal in the fat body, posterior silkgland and midgut.

• Animal cells and systems
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• v.2 no.3
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• pp.367-370
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• 1998

Two molecular species of apolipophorin-III (spoLp-III) were purified from the last instar larval hemolymph of Galleria mellonella by gel permeation chromatography (Sephadex G-100), ion exchange chromatography (DE-52), heat treatment (90C for 30 min) and Mono S FPLC, and were named apoLp-III-a and apoLp-lll-b, respectively. They were indistinguishable by SDS-PAGE but could be separated by native PAGE. The molecular mass of apoLp-III determined by SDS-PAGE was approximately 18 kDa. The N-terminal amino acid sequence of apoLp-III-b revealed high similarities with the apoLp-III from Manduca sexta.

• Proceedings of the Korean Society of Sericultural Science Conference
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• 2003.10a
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• pp.85-86
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• 2003

Apolipophorin III (apoLp-III) is a protypical exchangeable apolipoprotein that is abundant in hemolymph of many insect species. Its function lies in the stabilization of low-density lipophorin particles (LDLp) crossing the hemocoel in phases of high energy consumption to deliver lipids from the fat body to the flight muscle cells. But, recent studies with naive Galleria mellonella-apoLp-III gave first indications of an unexpected role of that protein in insect immune activation (Niere et al., 1999). (omitted)

• Proceedings of the Zoological Society Korea Conference
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• 1997.04a
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• pp.54.1-54
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• 1997

No Abstract, See Full Text

• Proceedings of the Korean Society of Sericultural Science Conference
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• 2001.04a
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• pp.60-60
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• 2001

No Abstract. See Full-text

• The Zoological Society Korea : Newsletter
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• v.12 no.2
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• pp.117.2-117
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• 1995