• 제목/요약/키워드: Haemolymph

검색결과 82건 처리시간 0.021초

누에 유충의 혈림프 유약호르몬 에스테라제 활성의 조절에 관한 연구 (Regulation of Haemolymph Juvenile Hormone Esterase Activity in Larvae of the Silkworm, Bombyx mori)

  • 손흥대;강필돈
    • 한국잠사곤충학회지
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    • 제34권1호
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    • pp.15-20
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    • 1992
  • 누에의 5령유충 섭식기 동안 절식, 두흉부 결찰, 재섭식 및 methoprene 등의 처리가 JHE 활성도의 조절에 미치는 영향을 실험한 바 그 결과는 다음과 같다. 1. 누에의 절식 및 결찰처리를 하면 혈림프 JHE 활성도가 감소하였다. 2. 절식누에는 재섭식에 의해 JHE 활성도가 증가하였으며, 재섭식에 의한 JHE 활성도의 증가시기는 절식기간에 따라 다르게 나타났다. 3. 절식누에에 methoprene을 투여하면 JHE 활성도는 5령 기잠과 1일에서는 변화가 없었으나 2일부터 5일에서 절식누에에 비해 1.3-1.4배 증가하였다. 4. 결찰누에에 methoprene을 처리하면 JHE 활성도는 5령 기잠에 변화가 없었고 1일부터 5일에서는 결찰누에에 비해 1.9-2.3배 증가하였다. 5. 이상의 결과에서 5령누에의 섭식기 동안 JHE 활성도의 조절에는 두부요인, JH 및 영양 등이 중요한 요인으로 작용하였다 .특히 섭식기에 있어서 JHE는 두부요인과 JH의 공동작용에 의해 조절되지만, 령의 초기에는 두부요인이 그 후에는 JH가 보다 중요한 역할을 하는 것으로 생각된다.

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누에의 變態에 따른 貯藏蛋白質의 出現과 分布에 관하여 (On the Occurrence and Distribution of Storage Proteins During the Metamorphosis of Bombyx mori L)

  • Eul Won Seo;Hak Ryul Kim
    • 한국동물학회지
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    • 제29권1호
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    • pp.1-12
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    • 1986
  • 누에의 變態期 동안 貯藏蛋白質의 出現과 번데기 시기동안 각 組織에 따른 貯藏蛋白質의 分布를 살펴보기 위해 電氣泳動法, 免疫學的 方法 및 column chromatography法을 使用하였다. 혈림프의 貯藏蛋白質은 2개로 區分이 되었고, 5령 初期부터 出現하고 있으며 지방체 단백질과도 동일한 전기영동상의 移動度를 갖고 있다. 이의 量的 變化는 終令期에는 혈림프에서 높은 濃度를 유지하다.  化後에는 脂肪體에 축적이 되는 경향을 나타내며 특히 저장단백질-2가 암수에서 모두 두드러진 저장단백질의 양상을 보이고 있다. 이러한 貯藏蛋白質은 종령 末期에는 큐리클 단백질 형성에도 관여하는 것 같으며 번데기에는 中腸도 일시적으로 저장단백질을 저장하는 것 같다. 또한 貯藏蛋白質中 저장단백질-2는 vitellogenin과 정기영동 및 면역학적으로 동일한 이동도를 나타내고 있으며 특히 번데기시기동안 卵黃蛋白質의 항체에 대해 항원-항체반응을 나타내고 있어 卵形成過程에도 밀접하게 관여하는 것 같다.

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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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담배나방의 휴면 용 혈림프 Carboxylesterase의 생화학적 특성 (Biochemical Properties of Haemolymph Carboxylesterase in Diapausing Pupae of Helicoverpa assulta (Guenee))

  • 김영관;이형철;박희윤;이옥경;유종명
    • 한국연초학회지
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    • 제20권1호
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    • pp.71-79
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    • 1998
  • Haemolyph carboxylesterases induced in diapausing pupae of Helicoverpa assulta Guenee were investigated. Increase in the activity of the electrophoresed isozyme bands were observed during the diapausing pupae. The isozymatic composition exhibited remarkable alterations represented as disappearance and induction of some isozyme bandsp which were identified as carboxylesterase (CE) on the basis of their specificities to inhibitors. Much higher activity of the induced CE was shown in reaction with $\beta$-naphthyl acetate ($\beta$-Na) than $\alpha$-naphthyl butyrate ($\alpha$-Nb), representing the high regioselectivity to $\beta$-naphthyl group. Optimal temperature for the enzyme activity was different to the substrates used 37$^{\circ}C$ in $\beta$-Na and 4$0^{\circ}C$ in $\alpha$-Nb, respectively. However, the optimal pH for the enzyme activity was the same as 7.5 regardless of the substrates used, and relatively high thermostability of the CE was demonstrated by showing the denaturation at high temperature (50~55$^{\circ}C$).

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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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