• Korean journal of applied entomology
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• v.37 no.1
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• pp.59-64
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• 1998

A juvenile hormone binding protein (JHBP) has been isolated from the whole body homogenate of Galleria rnellonella final instar larvae by gel filtration. The isolated protein is homogenous as judged by column chromatography and gel electrophoresis in the presence and absence of denaturing agent. The JHBP has a relative molecular weight of 32 k by denaturing gel electrophresis and 28 k by gel filtration. The protein exhibits a dissociation constant of 3.9 x M for JH 111.

• Proceedings of the Zoological Society Korea Conference
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• 1994.10a
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• pp.183.2-183
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• 1994

• Korean journal of applied entomology
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• v.43 no.2
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• pp.143-153
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• 2004

Non-spinning syndrome of Bombyx mori has been serious issue in sericulture industry near Kyungbuk area. This study was focused on the analysis of the mechanism and on screening candidate chemicals inducing the anti-metamorphosis of the silkworms. Rearing temperatures or initial body weight of the final instar larvae did not affect a normal larval to pupal metamorphosis of B. mori. However, pyriproxyfen (a juvenile hormone (JH) agonist) induced follicle patency significantly even at its 10$\^$-8/ M concentration and inhibited metamorphosis of B. mori in both developmental time and dose dependent manners. Pyriproxyfen induced JH esterase (JHE) activity and downregulated expression of JH binding protein of 5. mori. These results suggests that pyriproxyfen induced JHE activity as a JH agonist and that the elevated JHE activity degraded endogenous JH and resulted in JHBP gene expression. Based on the fact that the JH agonist induced follicle patency and inhibited metamorphosis of B. mori, follicle patency bioassay suggested that three commercial pesticides including simazine, molinate or alachlor were proved to give potent JH agonistic effect on B. mori. Further direct exposure experiments to these candidates are required to determine the chemicals responsible for the non-spinning syndrome of 8. mori.

• The Korean Journal of Zoology
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• v.37 no.1
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• pp.66-75
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• 1994

Juvenile hormone binding protein was identified in the hemolymph of fifth instar larvae and purified using column chromatography. Hemolymph was mixed with [3H] JH-III and electrophoresed on 691 NON-SDS gel, indicating that radioactivity peak appears at Rf value of 0.55. Gel filtration showed two radioactivity peaks equivalent to bound and free [3H]JH-III, respectively. JHBP was purified from hemolymph through gel filtration (Sephadex G-100), anion exchange chromatosraphv (DEAE Sepharose CL-6B), chromatofocusing chromatographv (PBE 94) and preparative electrophoresis.