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ID:33010847
大小:2.66 MB
页数:71页
时间:2019-02-19
《非离子型表面活性剂复合双水相体系与其蛋白质分配平衡分析》由会员上传分享,免费在线阅读,更多相关内容在行业资料-天天文库。
1、汕头大学硕士学位论文sizewouldaffectthepartitioningbehaviorofmodelproteins.TheresultshowsthattheproteinswithlowmolecularweightsuchasLYSandα-LAtendtoaggregateinPEGphase,thistendencywouldbeenhancedbyincreasingTLLofATPS.However,thepartitioningcoefficientofthehighermolecula
2、rweightproteinsuchasBSAandOVAdecreasedramatically.Moreover,withPEGmolecularweightrising,thepartitioningcoefficientwillreducesignificantly.Additionally,alltheselectedmodelproteinsarepartitionedpreferablyintothesalt-richphase,andthepartitioningcoefficientdecrea
3、sewithincreasingTLLinbothPEG/Na2SO4ATPSandTX-100/Na2SO4ATPS.(4)Thehydrophobicinteractionandexclude-volumeinteractionpartitioningmodelwasappliedtocorrelatethepartitioningcoefficientsofmodelproteins.TheresultsofqualitativeanalysesindicatethatthecontributionofTX
4、-100-richphaseforexclude-volumeinteractioninproteinpartitioningintheaqueoustwo-phasesystemscomposedofPEGandTX-100isstrongerthanPEG-richphase,andthetrendwouldbeenhancedbyincreasingTLLandlowerthePEGmolecularweight.Also,theeffectofhydrophobicinteractionmaketheta
5、rgetproteinpartitiontothebottomphase.HydrophobicresolutionofATPSincreaseswithincreasingTLLandPEGmolecularweightwhilethechangeofintrinsichydrophobicityisnotobvious.(5)ThePEG/TX-100aqueoustwo-phasesystemwasappliedinpartitioningofmembraneproteinseparationofHalob
6、acteriumhalobium.Theseparationofthemembraneproteinweremadebycomparingtheaqueoustwo-phasesystemandsucrosegradientcentrifugation.TheresultdemonstratedthatthetargetproteincouldpartitionintotheTX-100-richphase,andthecontaminantproteinswereextractedintothePEG-rich
7、phasebymulti-stageextractprocess.Keywords:aqueoustwo-phasesystems,polyethyleneglycol,TX-100,exclude-volumeinteraction,hydrophobicityinteractionIV万方数据汕头大学硕士学位论文目录摘要................................................................................................
8、.....................................IABSTRACT.....................................................................................................................III目录...................
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