• Journal of Sericultural and Entomological Science
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• v.34 no.1
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• pp.15-20
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• 1992

Effects of starvation, ligation, refeeding and methoprene treatment in the feeding phase of the fifth instar larvae of Bombyx mori on the regulation of juvenile hormone esterase(JHE) activity were investigated. Starvation and ligation contributed to the reduction of JHE activity, however, JHE levels in starved larvae were slightly higher than in legated larvae. Haemolymph JEH activity of starved larvae was increased by refeeding, and duration of increasing time of JHE activity after starvation was related to duration of starvation. When starved larvae were applied methoprene topically, JHE activity were not changed at day 0 and 1, but were increased by 1.3-1.4 times between day 2 and 5. When ligated larvae were applied methoprene topically, JHE activity was not changed at day 0, but were increased by 1.9-2.3 times between day 1 and 5. These results suggest that head factor, juvenile hormone(JH) and nutrient are major factors in the regulation of JHE in the feeding phase of the fifth instar larvae of Bombyx mori. Especially JHE might be regulated by the co-operative action of head factor and JH. However, head factor plays important role in the early stage, while JH plays important role thereafter.

• The Korean Journal of Zoology
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• v.29 no.1
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• pp.1-12
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• 1986

Electrophoretic, immunological, and column chromatography methods were used to determine the appearance and distribution of storage proteins in various organs during the metamorphosis of Bombyx mori L. Two storage proteins start to appear in haemolymph in early 5th instar stage and show the identical mobility with fat body proteins. These proteins show the high concentration in haemolymph in last instar stage but accumulate in fat body after pupation. Storage protein-2 shows the distinct pattern for general storage proteins in both male and females. This protein is involved with the formation of cuticle protein in late last instar stage and appears to be temperally deposited in midgut during the pupal stage. Also SP-2 shows the identity with vitellogenin electrophoretically and immunologically and especially the positive reaction with antibody against yolk protein during the pupal stage, demonstrating that the storage protein is closely related to the formation of yolk protein.

• Journal of the Korean Society of Tobacco Science
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• v.18 no.1
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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.

• Proceedings of the Korean Society of Sericultural Science Conference
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• 2001.10a
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• pp.72-72
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• 2001

no Abstract, See Full Text

• Proceedings of the Korean Society of Sericultural Science Conference
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• 2001.10a
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• pp.73-73
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• 2001

no Abstract, See Full Text

• Journal of the Korean Society of Tobacco Science
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• v.20 no.1
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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$^{\circ}C$).

• The Korean Journal of Zoology
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• v.34 no.3
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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.

• Animal cells and systems
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• v.3 no.1
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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.

• Proceedings of the Korean Society of Sericultural Science Conference
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• 2002.10a
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• pp.61-61
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• 2002

No Abstract, See Full Text

• Proceedings of the Korean Society of Sericultural Science Conference
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• 2002.10a
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• pp.60-60
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• 2002

No Abstract, See Full Text