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• W2109848198 abstract "Abstract Hirudin, isolated from the leech Hirudo medicinalis, inhibits thrombin directly and several expression systems have been used to produce recombinant Hirudin (rHirudin) for pharmaceutical purposes. A DNA fragment containing the Hirudin coding sequence and goat β‐casein secretion signal was chemically synthesized in this study. The synthetic DNA then was further constructed into a goat β‐casein expression vector for mouse transgenesis. Four lines of transgenic mice were successfully developed and one line showed a meaningful anti‐thrombin activity of 40,000 anti‐thrombin units (ATU)/mL in their milk. In this animal line, Hirudin mRNA was found in samples of uterus and kidney with insignificant anti‐thrombin activity (≤ 280 ATU/g wet tissue); however, mammary glands showed a higher activity of 780 ATU/g wet tissue. Transgenic mice showed no evident physical abnormality. The purified rHirudin was further analyzed by amino acid analysis and was found to contain a tyrosine O ‐sulfate residue that is absent in rHirudin expression either through Escherichia coli or yeast host systems. Experimental results demonstrated that the β‐casein‐promoted Hirudin transgene could be successfully expressed in a murine model and may be applicable to large mammals such as livestock for mass production of rHirudin for pharmaceuticals." @default.
• W2109848198 created "2016-06-24" @default.
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• W2109848198 date "2008-08-01" @default.
• W2109848198 modified "2023-10-16" @default.
• W2109848198 title "Expression of recombinant Hirudin in transgenic mice milk driven by the goat β-casein promoter" @default.
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• W2109848198 doi "https://doi.org/10.1002/biot.200800069" @default.
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