Abstract
For biophysical studies using heteronuclear NMR analysis of amyloid beta peptide, construction of an efficient and high yield expression system of uniformly isotopic labeled amyloid beta peptide is desirable. Here we succeeded in obtaining 15N-labeled amyloid beta 1-40 expressed by attachment to hen egg white lysozyme as a fusion protein.
Keywords: Alzheimer's disiease, amyloid β 1-40, amyloid fibrils, recombinant protein, Escherichia coli, NMR
Protein & Peptide Letters
Title: Expression and Purification of Uniformly 15N-Labeled Amyloid β Peptide 1-40 in Escherichia coli
Volume: 14 Issue: 8
Author(s): M. Nagata-Uchiyama, M. Yaguchi, Y. Hirano and T. Ueda
Affiliation:
Keywords: Alzheimer's disiease, amyloid β 1-40, amyloid fibrils, recombinant protein, Escherichia coli, NMR
Abstract: For biophysical studies using heteronuclear NMR analysis of amyloid beta peptide, construction of an efficient and high yield expression system of uniformly isotopic labeled amyloid beta peptide is desirable. Here we succeeded in obtaining 15N-labeled amyloid beta 1-40 expressed by attachment to hen egg white lysozyme as a fusion protein.
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Cite this article as:
M. Nagata-Uchiyama , M. Yaguchi , Y. Hirano and T. Ueda , Expression and Purification of Uniformly 15N-Labeled Amyloid β Peptide 1-40 in Escherichia coli, Protein & Peptide Letters 2007; 14 (8) . https://dx.doi.org/10.2174/092986607781483741
DOI https://dx.doi.org/10.2174/092986607781483741 |
Print ISSN 0929-8665 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5305 |
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