1.Comparison of carbohydrate moieties of sparganum proteins of the snake, mouse and those of adult worm.
The Korean Journal of Parasitology 2003;41(2):135-137
The carbohydrate moieties of larval sparganum proteins in two different species, the snakes, Elaphe rufodorsata, the Balb/c mouse and those of the adult worm, Spirometra erinacei, were compared using five different lectins including GNA, SNA, MAA, PNA and DSA. The GNA positive 53 kDa molecule, which is excretory-secretory protease in the sparganum from the snake showed a stage specific and developmental regulation. We also suggested that sparganum glycosylation may be involved in immune evasion and differentiation into an adult worm.
Animals
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Carbohydrates/*metabolism
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Comparative Study
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Glycoproteins/*metabolism
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Human
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Mice
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Mice, Inbred BALB C
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Snakes/*metabolism
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Sparganum/*metabolism
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Species Specificity
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Spirometra/*metabolism
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Support, Non-U.S. Gov't
2.Expression of human apolipoprotein A- I in baculovirus-insect cell system.
Yuan-E ZHU ; Hui-Bin XU ; Zhi-An ZHAO ; Jiang ZHONG
Chinese Journal of Biotechnology 2003;19(6):692-697
Apolipoprotein A- I is the major apolipoprotein in high-density lipoprotein known to have a wide range of physiological functions, the best-studied one of which is in regulating cholesterol metabolism and preventing arteriosclerosis. Human blood has been the only source of this protein. To facilitate further research and application, it is essential to produce it through genetic engineering. In the current research, the baculovirus-insect cell system was used to overexpress human apolipoprotein A- I . Two recombinant baculoviruses were constructed. The first one expressed a pro form of apoA- I lacking native signal peptide. The recombinant protein was found to remain mainly inside cells in the early phase of infection, while being largely excreted to the medium late in infection. The second one used a heterologous signal peptide, snake phospholipase A2 inhibitor alpha subunit signal peptide, to lead the secretion of mature apoA- I. In contrast to the first virus, recombinant apoA- I was found in the culture medium at the early phase of virus infection. The mature apoA- I was purified from culture medium using Phenyl Sepharose hydrophobic interaction chromatography (HIC) and eluted with water and Propylene. This work shows that snake phospholipase A2 inhibitor a subunit signal peptide can be used to secret human apoA- I in insect cells, but the efficiency of its secretion is limited when the expression level is high.
Animals
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Apolipoprotein A-I
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genetics
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metabolism
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Baculoviridae
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genetics
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Blood Proteins
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genetics
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metabolism
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Blotting, Western
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Cell Line
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Chromatography
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Genetic Vectors
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genetics
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Humans
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Recombinant Proteins
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genetics
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metabolism
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Snakes
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Spodoptera
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cytology