东北林蛙皮肤抗菌肽抗病毒活性的初步研究-动物学专业论文.docx

东北林蛙皮肤抗菌肽抗病毒活性的初步研究-动物学专业论文.docx

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东北林蛙皮肤抗菌肽抗病毒活性的初步研究-动物学专业论文

Abstract The skin antimicrobial peptides(AMPs)are the barrier for amphibians to defense invading of microorganism.They have many families and lots of functions,such as anti bacteria.anti fugin and anti tumor.Recently,it reported that AMPs have inactivate properties to herpes virus and HIV-1,and simultaneity no harm for host cells.Nowadays the spread of virus diseases depress the globle economy,to find safe,effective antiviral medicine became the focus.For the unique characters of amphibian skin peptides,it is hoped to be the important way of exploring new antibiotic. In this paper,we isolate and purified AMPs from northeast forest frogs(Raria dybowskii), choose the SAIl hydrolase as the antiviral filtration model tO determine the broad-spectrum antiviral properties,then choose the zoonosis virus -H9N2 avian influenza virus to investigate its inactive properties to enveloped virus. Result:(1)We extract and purified SAH hydrolas from bovine liver,the specific activity of the extract SAH hydrolase is 1.23U/mg,it can catalyse 30.7%Hey to SAH within 1 minute;(2)When put the skin peptide of Northeast forest frog into the reaction system.thefe is 44·7%Hey change into SAIl within 1 minute,It indicate that the skin peptide of Northeast forest frogs regress the activity of SAH hydrolase,which indicate that the skin activity peptide has broad-spectrum activity;(3)The maximum nontoxic concentration is 150mg/m1.there are comparison group,infection group,killing group,and therapy group and prevent group in this experiment·Compared with infection group,the titer of therapy group and prevent group,the killing group differ signiflcant(PO.01),the HA of killing guoup reduced from(10_+0.82)to(3 ±0·82),the HA of prevent group reduce by(5.5±0.50),HA of therapv group reduce to (5·3±O·58),compared with therapy group and prevent group,the killing group shows distinct effect on the avian influenza virus H9N2. Conclusion:(1)We establish antiviral filtration model in vitro .SAH hydrolase mQd

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