期刊
JOURNAL OF CHROMATOGRAPHY B-ANALYTICAL TECHNOLOGIES IN THE BIOMEDICAL AND LIFE SCIENCES
卷 856, 期 1-2, 页码 229-233出版社
ELSEVIER
DOI: 10.1016/j.jchromb.2007.06.003
关键词
purification; amyloid-beta peptide; cytotoxicity; aggregation; Alzheimer's disease
The amyloid cascade hypothesis assigns the amyloid-beta peptide (A beta) a central role in the pathogenesis of Alzheimer's disease (AD). Although there are strong efforts to biophysically characterize formation of A beta aggregates and fibrils, as well as their prevention, progress is still severly hampered by the availability of tens of milligrams of recombinant A beta(1-42). Here, we describe a reliable and easy procedure to recombinantly express and purify A beta(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. (C) 2007 Elsevier B.V. All rights reserved.
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