• 제목/요약/키워드: Haemolymph protein

검색결과 53건 처리시간 0.03초

담배나방 저장단백질 SP-2의 정제 및 생화학적 특성 (Purification and Biochemical Properties of Storage Protein SP-2 in Tobacco Budworm (Helicoverpa assulta Guenee))

  • 정성은;채순용;김선봉;이형철
    • 한국연초학회지
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    • 제18권1호
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    • pp.39-48
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    • 1996
  • A storage protein(SP-2) was confirmed in haemolymph during larval-pupal-adult development of tobacco burdworm(Helicoverpa assulta Guenee), and its biochemical characteristics were investigated. The titer of SP-2 showed a peak at mature larva, decreased gradually through the late pupal stage, and became undetectable at adult period. As the results from electrophoretic mnysis, SP-2 was confirmed to be glycolipoprotein(M.W. 332kDa) relatively stable to heat( $\leq$ 68$^{\circ}C$ ). This storage protein was determined to be a tetramer composed of a single subunit with MW of 83kDa, and the isoelectric point was 5.7. The amino acid composition of the SP-2 was characterized. It has relatively high content of methionine and histidine, whereas the contents of tyrosine and phenylalanine were relatively low.

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미국흰불나방(Hyphantria cunea D.)의 난황단백질-3의 합성 및 이용 (Synthesis and Fate of Yolk Protein-3 in Hyphantria cunea D.)

  • 이상대;김학열
    • 한국동물학회지
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    • 제34권3호
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    • pp.394-402
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    • 1991
  • Yolk protein-3 (YP3) was purified from the ovary of Hvpharatria cunea D. and the synthesis and fate during embryogenesis of WP3 were investisated by electrophoresis and fluorography. YP3 purified through gel slice and electrophoretic elution'was determined to have M. W. of 18 Kd and consist of one subunit. Haemolymph and fat body of male and female %were electrophoresed during vifellogenic stages to indentifv the vitellosenin in female. The result showed that there was no distinct difference in electrophoretic patterns betweerl male and female. However, tissue culture of fat body and maturing ovary indicated that YP3 was svuthesized by fat body. Aiso, vP3 in iaid eggs was maintained constant untii naut s artier oviposition and then decreased, indicating that YP3 was drastically used during late embryosenesis. However, a part of YP3 was present even in newly hatched first instar larvae.

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Characteristics of Antifreeze Protein-1 Induced during Low Temperature Acclimation in the Protaetia brevitarsis (Coleoptera; Cetonidae) Larva

  • Hyung Chul Lee;Chong Myung Yoo
    • Animal cells and systems
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    • 제3권1호
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    • pp.47-52
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    • 1999
  • Change of proteins was confirmed during low temperature acclimation of overwintering larva, and some biochemical characteristics of the induced antifreeze protein-1 (AFP-1) were investigated in Protaetia brevitarsis. As the freezing point depression by the action of induced AFPs, a considerable thermal hysteresis was observed in the haemolymph and in partially purified proteins. AFP-1 was purified from the cold acclimation larvae by ammonium sulfate precipitation ion exchange chromatography, gel permeation chromatography, and electroelution. The purified AFP-1 was determined to be a glycoprotein (approximately 320 kDa, pl 5.8) composed of a single type of subunit (80 kDa). The high contents of hydrophilic amino acids (Asp, Glu, Lys, Asn, Gln, Arg, Ser, Thr) were also confirmed, showing similarity with antifreeze proteins from other insects.

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솔나방의 變態에 따른 血蛋白質의 變化 (Studies on the Haemolymph Proteins during the Metamorphosis of the Pine Moth, Dendrolimus spectabilis Butler)

  • Yoo, Chong-Myung;Lee, Kyung-Ro
    • 한국동물학회지
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    • 제17권2호
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    • pp.81-92
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    • 1974
  • 山林害蟲인 솔나방(Dendrolimus spectabilis Butler)의 變態에 따른 血蛋白質의 變化를 調査하기 위하여 acrylamide gel 電氣永動法을 이용하여 測定한 結果는 다음과 같다. 1. 血蛋白質의 band는 移動度에 따라 22개(1-22)의 종류를 나타냈다. 2. 血蛋白質의 濃度는 band 數, 染色强度, 移動度를 가지고 비교할 때 stage에 따라서 定量的 差異를 나타내며, 幼蟲이 성장함에 따라 增加하였고, 終齡幼蟲에서 가장 높은 濃度를 나타냈다. 3. 血蛋白質의 band는 終齡幼蟲을 지나 幼蟲器官의 解消가 일어나는 용전기에서 減少하고, 成蟲器官의 新生이 시작되는 용후기에서 다시 增加하였다. 4. PAS 반응, toluidine, Sudan black을 이용한 조직화학적 반응결과 終齡幼蟲에서 가장 많은 glycoprotein, mucopolysaccharide, lipoprotein등이 검출되었다. 5. 脂肪體와 腸에 있어서도 血蛋白質의 band 數와 비슷한 特性을 나타내었고 濃度의 變化도 유사하였다.

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The Effects of Vitamin C on Biological, Biochemical and Economical Characteristics of the Silkworm, Bombyx mori L.

  • Etebari, Kayvan;Ebadi, Rahim;Matindoost, Leila
    • International Journal of Industrial Entomology and Biomaterials
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    • 제8권1호
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    • pp.81-87
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    • 2004
  • In order to investigate the effects of supplementary nutrients on silkworms, Bombyx mori, an experiment was conducted with ascorbic acid treatments. Dietary supplements of ascorbic acid 1, 2 and 3% were fed to silkworm larvae through 1st to 5th instar, The larvae were fed by mulberry loaves of Kokoso variety and the supplementary loaves were used once a day. These treatments resulted in a significant increase of biological parameters such as larval weight, the rate of food consumption and the approximate digestibility of the food. But the economical parameters such as cocoon weight and cocoon shell weight didnt show considerable difference compared to control. Dietary supplement of 2% ascorbic acid increased the larval weight by 7.8% and reached to 1.065g, which had the highest weight increase in the fourth day of 4th instar larvae. The percentage of daily weight increase in this group of larvae (79.01%) had significant difference compared with other treatments. The nutritional efficiency index in this group of larvae was better than others. Also the abundance of biochemical macromolecules such as glucose, cholesterol, triacylglycerol and urea in haemolymph of larvae fed by 2% ascorbic acid increased to become 29.75 (mg/㎗), 24 (mg/㎗), 75.4(mg/㎗) and 32.1(mg/㎗) respectively. But protein contents of haemolymph of larvae in each treatment were not significantly different. Since all the results achieved were not considerable either statistically or economically, this method could not be recommended to improve the sericultural parameters.

Purification and Characterization of Arylphorin of the Chinese Oak Silkmoth, Antheraea pernyi

  • Park, Snag-Bong;Kim, Jeong-Wha;Kim, Soohyun;Park, Nam-Sook;Jin, Byung-Rae;Hwang, Jae-Sam;Seong, Su-Il;Lee, Bong-Hee;Park, Eunju
    • International Journal of Industrial Entomology and Biomaterials
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    • 제6권1호
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    • pp.33-44
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    • 2003
  • The arylphorin was purified from the pupal haemolymph of the Chinese oak silkmoth, Antheraea pernyi, and characterized physiologically and biochemically, The protein was purified by a simple preparative polyacrylamide gel electrophoresis (PAGE) and subsequent diffusive elution. The preparation was shown to be homogeneous by 7.5% native-PAGE. The native molecular weight of arylphorin was 450 kDa with a 80 kDa single subunit, suggesting hexamer, The protein contained high amounts (18.3%) of aromatic amino acids, phenylalanine (9.7%) and tyrosine (8.6%). Therefore, the protein was identified as a kind of a storage protein referred to as an arylphorin. The protein was stained by Schiff's reagent, suggesting a glycoprotein. The protein contained 4.9% (w/w) sugar and mannose and N-acetylglucosamine were major components. Also, degradation of the protein was begun by heat treatment at 90 for 20 minutes. These results showed that the A. pernyi arylphorin in the study is hexamer associated with the six subunits consisting of a 80kDa single subunit, and is different from that of Kajiura et al. (1998) in the subunit composition.