000030237 001__ 30237
000030237 005__ 20200402210517.0
000030237 0247_ $$2DOI$$a10.1016/S1570-0232(02)00731-6
000030237 0247_ $$2WOS$$aWOS:000181406500006
000030237 037__ $$aPreJuSER-30237
000030237 041__ $$aeng
000030237 082__ $$a540
000030237 084__ $$2WoS$$aBiochemical Research Methods
000030237 084__ $$2WoS$$aChemistry, Analytical
000030237 1001_ $$0P:(DE-HGF)0$$aPreußer, A.$$b0
000030237 245__ $$aPurification of recombinantly expressed human cluster determinant 4 cytoplasmatic domain
000030237 260__ $$aNew York, NY [u.a.]$$bScience Direct$$c2003
000030237 300__ $$a39 - 44
000030237 3367_ $$0PUB:(DE-HGF)16$$2PUB:(DE-HGF)$$aJournal Article
000030237 3367_ $$2DataCite$$aOutput Types/Journal article
000030237 3367_ $$00$$2EndNote$$aJournal Article
000030237 3367_ $$2BibTeX$$aARTICLE
000030237 3367_ $$2ORCID$$aJOURNAL_ARTICLE
000030237 3367_ $$2DRIVER$$aarticle
000030237 440_0 $$03155$$aJournal of Chromatography B$$v786$$x1570-0232
000030237 500__ $$aRecord converted from VDB: 12.11.2012
000030237 520__ $$aA DNA fragment coding for the human CD4 cytoplasmic domain (residues 394-433) was cloned into the pET15b expression vector. The resulting plasmid was used for synthesis of the polyhistidine-tagged 5.10(3) M-r CD4 peptide in Escherichia coli BL21(DE3)Star. The CD4 cytoplasmic domain was purified under denaturing and reducing conditions by a two-step procedure using immobilized metal affinity chromatography and gel permeation chromatography. The purified CD4 cytoplasmic domain is soluble and functional without any specific refolding steps. The yield of the described purification procedure was similar to5 mg peptide per liter culture volume. (C) 2002 Elsevier Science B.V. All rights reserved.
000030237 536__ $$0G:(DE-Juel1)FUEK255$$2G:(DE-HGF)$$aNeurowissenschaften$$cL01$$x0
000030237 588__ $$aDataset connected to Web of Science
000030237 650_7 $$2WoSType$$aJ
000030237 65320 $$2Author$$apurification
000030237 65320 $$2Author$$aEscherichia coli
000030237 65320 $$2Author$$acluster determinant 4
000030237 7001_ $$0P:(DE-HGF)0$$aJonas, G.$$b1
000030237 7001_ $$0P:(DE-Juel1)132029$$aWillbold, D.$$b2$$uFZJ
000030237 773__ $$0PERI:(DE-600)1491259-4$$a10.1016/S1570-0232(02)00731-6$$gVol. 786, p. 39 - 44$$p39 - 44$$q786<39 - 44$$tJournal of chromatography / B$$v786$$x1570-0232$$y2003
000030237 8567_ $$uhttp://dx.doi.org/10.1016/S1570-0232(02)00731-6
000030237 909CO $$ooai:juser.fz-juelich.de:30237$$pVDB
000030237 9131_ $$0G:(DE-Juel1)FUEK255$$bLeben$$kL01$$lFunktion und Dysfunktion des Nervensystems$$vNeurowissenschaften$$x0
000030237 9141_ $$y2003
000030237 915__ $$0StatID:(DE-HGF)0010$$aJCR/ISI refereed
000030237 9201_ $$0I:(DE-Juel1)VDB58$$d31.12.2006$$gIBI$$kIBI-2$$lBiologische Strukturforschung$$x0
000030237 970__ $$aVDB:(DE-Juel1)27786
000030237 980__ $$aVDB
000030237 980__ $$aConvertedRecord
000030237 980__ $$ajournal
000030237 980__ $$aI:(DE-Juel1)ISB-2-20090406
000030237 980__ $$aUNRESTRICTED
000030237 980__ $$aI:(DE-Juel1)ICS-6-20110106
000030237 981__ $$aI:(DE-Juel1)IBI-7-20200312
000030237 981__ $$aI:(DE-Juel1)ISB-2-20090406
000030237 981__ $$aI:(DE-Juel1)ICS-6-20110106