• The Korean Journal of Zoology
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• v.34 no.1
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• pp.1-7
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• 1991

Lipophorin of Lymuntrn'adispor L. has been purified by KBr density gradient ultracentrifugation. The properties and synthetic site of lipophorin and quantitative change of lipophorin during development have been determined using electrophoresis and immunological analysis. Lipophorin is composed of ho subunits. apo-Lpl (230.000), ago-Lpll (49,000). ann contains carbohydrates and lipids. Anti-lipophorin showed positive reactions with fat body extract and ovary extract but not with gut extract. The concentration of lipophorin in hemolymph showed gradual decrease during larval and pupal stages. Also. fat body released lipophorin into medium. Immunological test showed some partial identity between lipophorin of Lymantpia dispar and hemolymph proteins (probably lipophorin) of Hyphontria cuneo and Galleria metlonefla.

• The Korean Journal of Zoology
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• v.37 no.1
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• pp.76-87
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• 1994

High density lipophorin-L (HDLP-L) was purified from the hemolymph of Bombyx modi using KBr density gradient ultracentrifugation and gel permeation chromatographv (Sephadex G-2001. Lipophorin has native molecular weight of 730 Nd and consists of Apo-Lp I and Apo-Lp II with molecular weights of 250 Kd and 90 Kd, respectively. Lp contains large amounts of glutamine & glutamic acid, threonine, leucine but small amounts of cysteic acid & oxidized cystine, tyrosine, methionine. Lp also contains diacylglycerol, cholesterol, phosphatidylcholine, and phosphatidylethanolamine. Anti-lipophorin showed positive reaction with fat body and ovarial extracts and also revealed immunological identity with lipophorin of Fall webworm, Hyphantria cunea. Lipophorin maintains constant level during larval and pupal stapes but greatlv increases during adult stage in both male and female. Apo-Lp III was purified from adult hemolymph. Hemolymph was subjected to KBr ultracentrifusation and Lp-free fraction was submitted to cation exchange chromatosraphy after ammonium sulfate precipitation. Apo-Lp III has molecular weight of 17 Kd, and similar amino acid composition ar those of other species Lp but contains high amounts of tryptophan which other are tacking in.

• The Korean Journal of Zoology
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• v.36 no.2
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• pp.231-237
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• 1993

Lipophorin (LP) was purified from hemolvmph of late last instar larvae of Hyphuntria cuneo D. by KBr density gradient ultracentrifugation. Chemical composition of LP was investigated by electrophoresis, thin laver chromatography and ryas chromatography. LP consisted of Apo-LP I and Apo-LP ll, and M.W. of them were 230 Kd and 80 Nd, respectivelv. Lipid of LP was mostly composed of neutral lipid including triacylglvcerol, diacvlslvcerol, monoacylglvcerol and free cholesterol, and phospholipid rich in phosphatidvlethanolamine and phosphatidvlcholine. Fatty acids present in these lipids were found to have be 14:0, 16:0, 18:1, and 20:1.

• Journal of the Korea Academia-Industrial cooperation Society
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• v.12 no.4
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• pp.1770-1774
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• 2011

This paper was to characterize the transfer of diacylglycerol(DAG) from lipophorin to Manduca sexta larval fat bodies. $[^3H]$-DAG-labeled Lp($[^3H]$-DAG-Lp) was incubated with the larval fat bodies under different times and the time of DAG transfer was determined. Incubation of fat bodies with $[^3H]$-DAG-Lp resulted in accumulation of DAG and TAG in the tissue. The transfer of $[^3H]$-DAG was inhibited in the presence of suramin and unlabeled lipophorin, which would be consistent with a lipophorin receptor. The effects of suramin may be complex because it can change membrane properties when bound to the lipophorin receptor and affect the rate of DAG transfer. To investigate the lipid uptake via receptor-mediated endocytosis, we treated with endocytosis inhibitors, ammonium chloride and chloroquine. The results show that the transfer process of lipid by lipophorin and fat bodies is receptor-mediated endocytosis.

• Proceedings of the Korean Society of Sericultural Science Conference
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• 2001.10a
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• pp.21-23
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• 2001

no Abstract, See Full Text

• 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.

• Proceedings of the Korean Society of Applied Entomolohy Conference
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• 2002.11a
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• pp.124-124
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• 2002

• Proceedings of the Zoological Society Korea Conference
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• 2003.08a
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• pp.175.3-175
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• 2003

No Abstract, See Full Text

• Proceedings of the Korean Society of Applied Entomolohy Conference
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• 2001.05a
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• pp.111-111
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• 2001

• Proceedings of the Korean Society of Applied Entomolohy Conference
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• 2001.11a
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• pp.113-113
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• 2001