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Purification of Rubisco activase from leaves or after expression in Escherichia coli

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<mark>Journal publication date</mark>7/03/2011
<mark>Journal</mark>Methods in Molecular Biology
Volume684
Number of pages12
Pages (from-to)363-374
Publication StatusPublished
Early online date24/09/10
<mark>Original language</mark>English

Abstract

Rubisco activase is a molecular chaperone that modulates the activation state of Rubisco by catalyzing the ATP-dependent removal of tightly-bound inhibitory sugar-phosphates from Rubisco's catalytic sites. This chapter reports methods developed for the purification of native and recombinant Rubisco activase from leaves and bacterial cells, respectively.