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Autographa Nuclear Polyhedrosis Virus (AcMNPV) Pk-1 Gene Structure And Its Kinase Activity Analysis

Posted on:2011-12-03Degree:MasterType:Thesis
Country:ChinaCandidate:K GuoFull Text:PDF
GTID:2120360305988528Subject:Biochemistry and Molecular Biology
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Kinase activity is pk-1 gene important biological activity. In this study, AcMNPV pk-1 gene expression and its different truncated sequence of the level of protein kinase activity, which reached the domain of the gene which features on the protein phosphorylation is required; To further clarify the baculovirus pk-1 gene virus replication in the function and regulation of gene expression in its most advanced mechanism basis.In studying, we find that the pk-1 gene and its deletions which is expressed by rosetta expression system have measurable phosphorylation.According to the analysis of Prosite database, we deduce:PK-1 protein has measurable phosphorylation, the series of 51-183 may be its functional region, this region is necessary to its phosphorylation.Meanwhile, pk-1 gene and its deletions has no valuable measurement about their autophosphorylation.This thesis contains four chapters. In chapter one, we present a brief introduction about baculovirus,including the classification status,replication,structures and VAPK.We also introduce the baculoviral application and the purpose of this study.In chapter two, we clone the pk-1 gene and its deletions into pMAL-c2x vector, meanwhile,we analysis the amino acid sequence of pk-1 gene in bioinformatics, finding associated functional region,which is important to make sure the essential functional region.In chapter three, we make sure the expression,purification and analysis of phosphorylation about pk-1 gene and its deletions, and forcast the region of essentiality.In chapter four, we summarize and discuss the result of this experiment , making a view of further studying.
Keywords/Search Tags:Baculovirus, AcMNPV, pk-1 gene, series of deletion, affinity purification, kinase activity, rosetta expression system
PDF Full Text Request
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