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@ARTICLE{Preuer:30237,
author = {Preußer, A. and Jonas, G. and Willbold, D.},
title = {{P}urification of recombinantly expressed human cluster
determinant 4 cytoplasmatic domain},
journal = {Journal of chromatography / B},
volume = {786},
issn = {1570-0232},
address = {New York, NY [u.a.]},
publisher = {Science Direct},
reportid = {PreJuSER-30237},
pages = {39 - 44},
year = {2003},
note = {Record converted from VDB: 12.11.2012},
abstract = {A 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.},
keywords = {J (WoSType)},
cin = {IBI-2},
ddc = {540},
cid = {I:(DE-Juel1)VDB58},
pnm = {Neurowissenschaften},
pid = {G:(DE-Juel1)FUEK255},
shelfmark = {Biochemical Research Methods / Chemistry, Analytical},
typ = {PUB:(DE-HGF)16},
UT = {WOS:000181406500006},
doi = {10.1016/S1570-0232(02)00731-6},
url = {https://juser.fz-juelich.de/record/30237},
}