TY  - JOUR
AU  - Wiesehan, K.
AU  - Funke, S. A.
AU  - Fries, M.
AU  - Willbold, D.
TI  - Purification of recombinantly expressed and cytotoxic human amyloid-beta peptide
JO  - Journal of chromatography / B
VL  - 856
SN  - 1570-0232
CY  - New York, NY [u.a.]
PB  - Science Direct
M1  - PreJuSER-60107
SP  - 229 - 233
PY  - 2007
N1  - Record converted from VDB: 12.11.2012
AB  - The amyloid cascade hypothesis assigns the amyloid-beta peptide (Abeta) a central role in the pathogenesis of Alzheimer's disease (AD). Although there are strong efforts to biophysically characterize formation of Abeta aggregates and fibrils, as well as their prevention, progress is still severly hampered by the availability of tens of milligrams of recombinant Abeta(1-42). Here, we describe a reliable and easy procedure to recombinantly express and purify Abeta(1-42), which is fully cytotoxic and able to form fibrils without any further refolding steps. The yield of the procedure is 5-8 mg of tag-less peptide per liter culture volume.
KW  - Amino Acid Sequence
KW  - Amyloid beta-Peptides: isolation & purification
KW  - Amyloid beta-Peptides: pharmacology
KW  - Base Sequence
KW  - Chromatography, High Pressure Liquid
KW  - DNA Primers
KW  - Humans
KW  - Molecular Sequence Data
KW  - Peptide Fragments: isolation & purification
KW  - Peptide Fragments: pharmacology
KW  - Recombinant Proteins: isolation & purification
KW  - Recombinant Proteins: pharmacology
KW  - Amyloid beta-Peptides (NLM Chemicals)
KW  - DNA Primers (NLM Chemicals)
KW  - Peptide Fragments (NLM Chemicals)
KW  - Recombinant Proteins (NLM Chemicals)
KW  - amyloid beta-protein (1-42) (NLM Chemicals)
KW  - J (WoSType)
LB  - PUB:(DE-HGF)16
C6  - pmid:17606418
UR  - <Go to ISI:>//WOS:000249615100032
DO  - DOI:10.1016/j.jchromb.2007.06.003
UR  - https://juser.fz-juelich.de/record/60107
ER  -