• 한국동물학회지
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• 제37권4호
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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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• 제3권2호
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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.

• 한국산학기술학회논문지
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• 제14권8호
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• pp.4106-4110
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• 2013

아포리포포린-III (apoLp-III)를 꿀벌부채명나방 종령 유충 혈림프에서 KBr 농도구배 초원심분리와 겔크로마토그래피 (Sephadex G-100)를 이용하여 분리, 정제하였다. 본 연구에서는 아포리포포린-III가 꿀벌부채명나방의 종령 유충 지방체에 의해 흡수되는 지를 조사하였다. 종령 유충 지방체 조직을 FITC로 표지한 아포리포포린-III(FITC-apoLp-III)와 상온에서 30분간 배양하였다. 배양 후 형광현미경과 전기영동을 이용하여 FITC-apoLp-III가 지방체 조직으로 들어가는 지의 여부를 확인하였다. 그 결과 FITC-apoLp-III가 유충 지방체로 흡수된다는 사실을 알 수 있었다.

• 한국산학기술학회논문지
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• 제10권3호
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• pp.620-624
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• 2009

아포리포포린-III를 꿀벌부채명나방 종령유충 혈림프에서 젤크로마토그래피 (Sephadex G-100)와 이온교환크로마토그래피 (CM-52)방법을 이용하여 분리, 정제하였다. 본 연구에서는 아포리포포린-III가 꿀벌부채명나방의 성충난소에 의해 흡수되는 지를 조사하였다. 성충난소조직을 형광물질로 표지한 아포리포포린-III와 상온에서 30분간 배양하였다. 배양결과를 형광현미경과 전기영동을 이용하여 확인한 결과 형광물질로 표지된 아포리포포린-III가 성충난소로 흡수된다는 사실을 알았다.

• International Journal of Industrial Entomology and Biomaterials
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• 제7권2호
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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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• 제2권3호
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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.

• 한국잠사학회:학술대회논문집
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• 한국잠사학회 2003년도 International Symposium of Silkworm/Insect Biotechnology and Annual Meeting of Korea Society of Sericultural Science
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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)

• 한국동물학회:학술대회논문집
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• 한국동물학회 1997년도 공동 춘계학술대회
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• pp.54.1-54
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• 1997

No Abstract, See Full Text

• 한국잠사학회:학술대회논문집
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• 한국잠사학회 2001년도 제44회 춘계 학술연구 발표자료
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• pp.60-60
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• 2001

No Abstract. See Full-text

• 한국동물학회:뉴스레터
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• 제12권2호
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• pp.117.2-117
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• 1995