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KMID : 0380219930260040317
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Journal of Biochemistry and Molecular Biology
1993 Volume.26 No. 4 p.317 ~ p.322
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Purification and Characterization of Juvenle Hormone Binding Protein from Hemolymph of Hyphantria
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In Hee Lee and Hak Ryul Kim
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Abstract
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Juvenile hormone binding protein (JHBP) was purified from hemolymph of last instar larvae by anion exchange chromatography, gel filtration and FPLC chromatofocusing chromatography. Also, dextran coated charcoal (DCC) binding assay (Engelmann, 1981) was employed to monitor the location of JHBP in chromatographic profile during the purification process. Purified JHBP was applied to SDS PAGE with standard molecular weight markers, indicating that JHBP has M.W. of 32 kD. And the value of isoelectric point was to be 5.3.
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KEYWORD
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