Expression and Purification of the Major Outer Membrane Protein of Chlamydia Trachomatis in Prokaryotic Cell-中国期刊网

摘要 Tocloneandconstructtherecombinantplasmidcontainingthemajoroutermembraneprotein(MOMP)geneofChlamydiatrachomatis(C.trachomatis)andtoexpressthefusionproteininE.coliBL21,theMOMPgenewasamphfiedbypolymerasechainreaction(PCR)fromgenomeofC.trachomatisserovarD.ThefragmentwasclonedintotheprokaryoticexpressionvectorpET-22b(+)afterdigestionwithBamHⅠandNotⅠandtransformedintoE.coliXL1-Blue.RecombinantswereselectedbyenzymedigestionandsequencingandtherecombinantplasmidwithMOMPgenewasthentransformedintoE.coliBL21withIPTGtoexpressthetargetgene.TheexpressionrecombinantproteinswerepurifiedbyNi-NTAaffinitychromatography,andidentifiedbySDS-PAGEandWesternblot.Itwasfoundthata1.2kbMOMPgenewasisolated.TheDNAsequenceofMOMPwasfoundtobejustthesameasthesequencepublishedbyGenBank.ArecombinantplasmidcontainingMOMPgenewasconstructedtoexpressthefusionproteinsinE.coli.SDS-PAGEanalysisshowedthattherelativemolecularweightoftherecombinantproteinwasabout47kDathatwasconsistentwiththetheoreticalpredictedvalue,andthespecificityoftheexpressedproteinwasconformedbyWesternblot.ItconcludedthattheMOMPgenecouldbeexpressedintheprokaryoticsystem,bywhichitprovidedthefoundationforthefuturestudiesonthebiologicalactivitiesofC.trachomatisandforthedevelopmentofvaccineagainstthispathogen.

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Expression and Purification of the Major Outer Membrane Protein of Chlamydia Trachomatis in Prokaryotic Cell

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Expression and Purification of the Major Outer Membrane Protein of Chlamydia Trachomatis in Prokaryotic Cell

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