1.The Design of Chinese Herbal Medicine Information Base Framework
Journal of Zhejiang Chinese Medical University 2006;0(05):-
For appeasement of far-line teaching of Chinese Traditional Medicine,multifunction searching Chinese Herbal medicine information glean.The system editor by C# language is a good terrace structure for collecting and demanding digital Chinese Herbal medicine.The thesis introduced a database import system based on web information extracted.The Brower/Server structure has a good extension and compatiblility in different data sources,can manage the visiting base from different data sources,can update the medicine information on line,can let thousands of user call on the system in the same time.The management system of Chinese Herbal medicine information based on WEB technology is an effective road to Chinese Herbal medicine information digital.
2.Effect of Tianyizhike Syrup on dispelling phlegm and relieving asthma
Guiyuan LU ; Pingfan LAI ; Chunlei FAN ; Kangke SHEN ; Senlin SHI ; Weihong GE
Chinese Traditional and Herbal Drugs 1994;0(04):-
Object To observe the effect of Tianyizhike Syrup on dispelling phlegm and relieving asthma. Methods The phenol red secreting tests in mice, capillary method in rats, asthma induced by spraying and trachea screwy strip method on guinea pig were adopted for observing the related pharmacological effect in different doses of Tianyizhike Syrup. Results Tianyizhike Syrup could obviously increase the amount of the mice secreting phenol red and the rat dispelling phlegm, prolong the latent period of the guinea pig asthma and significantly enlarge the bronchia smooth muscle. Conclusion Tianyizhike Syrup has a significant effect of dispelling phlegm and relieving asthma.
3.Expression in Escherichia coli, purification and enzymatic properties of chicken aminopeptidase H.
Qingan LAI ; Shutao LIU ; Wanhua LU ; Li CHEN ; Toshihide NISHIMURA ; Pingfan RAO
Chinese Journal of Biotechnology 2008;24(3):381-386
Aminopeptidase H (APH) is an universally distributed aminoendopeptidase in the tissue of many organism. However, it is hard to investigate its mechanism underlying the catalysis and the function in cell. In this paper, the full DNA sequence of this enzyme was cloned from chicken liver, then subcloned to the vector pET22 b(+). The recombined vector was transformed into E. coli Rosetta(DE3), and the APH gene was expressed by the induction of IPTG. It was found the recombinant protein exhibited same mo lecular weight as authentic APH on SDS-PAGE analysis; the expression level increased with induction time and approached maximum of 94.7 mg/L till 6 hours, which contained 16.7% of the total protein. Moreover, this recombinant protein showed similar prop erties of subunit composition, thermal stability and optimum pH with native APH, based on the enzymatic assay, purification and analysis of enzymological properties. Therefore, it is confirmed that APH was expressed in this prokaryote system with a high-level of 1636 u/L aminopeptidase activity. These results would help to elucidate the catalysis mechanism and biological function of APH by providing enough material.
Aminopeptidases
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biosynthesis
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genetics
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Animals
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Chickens
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Endopeptidases
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biosynthesis
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genetics
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Enzyme Stability
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Escherichia coli
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genetics
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metabolism
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Recombinant Proteins
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biosynthesis
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genetics
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isolation & purification