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KMID : 0613820070170081046
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Journal of Life Science
2007 Volume.17 No. 8 p.1046 ~ p.1052
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Characterization and Distribution of Transferrin from the Last Larval Haemolymph of Papilio xuthus
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Shin Myung-Ja
Kim Kyoung-Keun
Kim Jeong-Sook
Lim Jae-Hwan
Seo Eul-Won
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Abstract
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Transferrin is a molecule carrying iron to store and maintain for iron homeostasis of living organisms. In this study, we have purified transferrin, as an iron-binding protein, from the last larval haemolymph of Papilio xuthus by KBr density gradient ultracentrifugation and gel filtration (superose 6 HR) using fast protein liquid chromatography (FPLC) and transferrin containing iron was identified by Ferene S staining. The purified haemolymph transferrin was shown to have molecular mass of 78 and 80 kDa and amino acid composition of transferrin was rich in aspartic acid, valine, leucine and glutamic acid. With immuno-diffusion assay, we confirmed the existence of the transferrin in the haemolymph and fat body by detection of visible and clear positive reaction. From the quantitative comparison by rocket immuno-electrophoresis process, the amount of transferrin were increased in the haemolymph of 3 days after pupation and the whole 5 days after pupation. Here, with biochemical and immunohistochemical analysis, we speculate the relationship of transferrin between the physical characteristics and distribution during metamorphosis of P. xuthus.
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KEYWORD
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Papilio xuthus, haemolymph, fat body, transferrin
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