Aβ produced as a fusion to maltose binding protein can be readily purified and stably associates with copper and zinc

Protein and Peptide Letters

Volumn 14, Issue 1, 2007, Pages 83-86

  Caine, J ^a   Volitakis, I ^b,c   Cherny, R ^b,c   Varghese, J ^a   Macreadie, I ^a  

^a CSIRO   (Australia)

^b FLOREY INSTITUTE OF NEUROSCIENCE AND MENTAL HEALTH   (Australia)

^c UNIVERSITY OF MELBOURNE   (Australia)

Author keywords

Alzheimer's disease; Amyloid peptide; Copper binding; Zinc binding

Indexed keywords

ESCHERICHIA COLI;

AMYLOID BETA PROTEIN; AMYLOID BETA PROTEIN (1 42); AMYLOID BETA-PROTEIN (1-42); CARRIER PROTEIN; COPPER; HYBRID PROTEIN; MALTOSE BINDING PROTEIN; MALTOSE-BINDING PROTEIN; PEPTIDE FRAGMENT; UNCLASSIFIED DRUG; ZINC;

AMINO ACID SEQUENCE; ARTICLE; BIOSYNTHESIS; ENZYME STABILITY; GENETICS; ISOLATION AND PURIFICATION; METABOLISM; MOLECULAR GENETICS;

AMINO ACID SEQUENCE; AMYLOID BETA-PROTEIN; CARRIER PROTEINS; COPPER; ENZYME STABILITY; MOLECULAR SEQUENCE DATA; PEPTIDE FRAGMENTS; RECOMBINANT FUSION PROTEINS; ZINC;

EID: 33845967502     PISSN: 09298665     EISSN: None     Source Type: Journal    
DOI: 10.2174/092986607779117263     Document Type: Article

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