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

Caine, J, Volitakis, I, Cherny, R, Varghese, J and Macreadie, I 2007, 'Abeta produced as a fusion with maltose binding protein can be readily purified and stably associates with copper and zinc ', Protein and Peptide Letters , vol. 14, no. 1, pp. 83-86.


Document type: Journal Article
Collection: Journal Articles

Title Abeta produced as a fusion with maltose binding protein can be readily purified and stably associates with copper and zinc
Author(s) Caine, J
Volitakis, I
Cherny, R
Varghese, J
Macreadie, I
Year 2007
Journal name Protein and Peptide Letters
Volume number 14
Issue number 1
Start page 83
End page 86
Total pages 4
Publisher Bentham Science Publishers Ltd.
Abstract The 42 amino acid Alzheimer's AP peptide has been produced in E. coli as a soluble fusion to maltose binding protein (MBP). Affinity purification on amylose columns of MBP-Ap and MBP led to the recovery of proteins at purities that were suited for physicochemical analyses. MBP-Ap was able to bind approximately 2 mole equivalents of copper or 4 mole equivalents of zinc, while MBP alone bound negligible amounts of zinc or copper. We conclude that AP can bind 2 copper or 4 zinc ions in its fusion format. Because MBP-Ap is a convenient protein to work with, this system is well suited for further studies on the structure of AP and its interactions with metals.
Subject Medicinal and Biomolecular Chemistry not elsewhere classified
Keyword(s) Alzheimer's disease
amyloid peptide
copper binding
zinc binding
Copyright notice © 2007 Bentham Science Publishers Ltd.
ISSN 0929-8665
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