Expression and purification of uniformly (15)N-labeled amyloid beta peptide 1-40 in Escherichia coli.
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 (15)N-labeled amyloid beta 1-40 expressed by attachment to hen egg white lysozyme as a fusion protein.
Nagata-Uchiyama
M
M
Graduate School of Pharmaceutical Sciences, Kyushu University, 3-1-1 Maidashi, Higashiku, Fukuoka, Japan.
Yaguchi
M
M
Hirano
Y
Y
Ueda
T
T
D000595:Amino Acid Sequence; D016229:Amyloid beta-Peptides / Q000096:biosynthesis* / Q000302:isolation & purification; D004926:Escherichia coli / Q000378:metabolism; D007553:Isotope Labeling / Q000379:methods; D008969:Molecular Sequence Data; D009113:Muramidase / Q000378:metabolism; D009587:Nitrogen Isotopes; D019906:Nuclear Magnetic Resonance, Biomolecular; D010446:Peptide Fragments / Q000096:biosynthesis* / Q000302:isolation & purification; D011993:Recombinant Fusion Proteins / Q000096:biosynthesis; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
D016229:Amyloid beta-Peptides; D009587:Nitrogen Isotopes; D010446:Peptide Fragments; D011993:Recombinant Fusion Proteins; C078592:amyloid beta-protein (1-40); D009113:Muramidase