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Affinity Capillary Electrophoresis: Study of the Binding of HIV-1 gp41 with a Membrane Protein (P45) on the Human B Cell Line, Raji
作者姓名:王清刚  罗国安  吴伟成  陈应华
作者单位:WANG Qinggang(王清刚),LUO Guoan(罗国安),WU Weicheng(吴伟成),CHEN Yinghua(陈应华) Department of Chemistry,Tsinghua University,Beijing\ 100084; Department of Biological Sciences and Biotechnology,Tsinghua University,Beijing\ 100084
摘    要:IntroductionSincethediscoveryofHIV1,theaetiologicalagentofAIDS[1],therehasbeenincreasinginterestintheinteractionofHIVenvelop...


Affinity Capillary Electrophoresis:Study of the Binding of HIV-1 gp41 with a Membrane Protein (P45) on the Human B Cell Line,Raji
WANG Qinggang,LUO Guoan,WU Weicheng,CHEN Yinghua.Affinity Capillary Electrophoresis: Study of the Binding of HIV-1 gp41 with a Membrane Protein (P45) on the Human B Cell Line, Raji[J].Tsinghua Science and Technology,1999,4(2).
Authors:WANG Qinggang  LUO Guoan  WU Weicheng  CHEN Yinghua
Abstract:Affinity capillary electrophoresis has been used to study the interaction between a membrane protein (P45) isolated from the Human B cell line, Raji, and rsgp41. P45, rsgp41 and the complexes were well resolved. The entire separation was achieved in less than 3min. Formations of two kinds of stable P45 rsgp41 complexes were confirmed based on migration time comparison; the binding equilibrium was achieved as soon as two proteins were mixed. The results indicate that the interaction between P45 and rsgp41 is strong with a fast association rate and a slow dissociation rate, and there are at least two kinds of binding sites with different binding constants between P45 and rsgp41.
Keywords:affinity capillary electrophoresis  HIV-1 gp41  membrane protein
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