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. 1988 Aug;87(4):917–920. doi: 10.1104/pp.87.4.917

Catalysis of Ribulosebisphosphate Carboxylase/Oxygenase Activation by the Product of a Rubisco Activase cDNA Clone Expressed in Escherichia coli

Jeffrey M Werneke 1,2, J Mark Chatfield 1,2, William L Ogren 1,2
PMCID: PMC1054869  PMID: 16666245

Abstract

Ribulose-1,5-bisphosphate carboxylase/oxygenase (rubisco) activase activity was obtained from a partially purified extract of Escherichia coli transformed with a 1.6-kilobase spinach (Spinacia oleracea L.) cDNA clone. This activity was ATP-dependent. Catalysis of rubisco activation by spinach and cloned rubisco activase was accompanied by the same extent of carboxyarabinitol bisphosphate-trapped 14CO2 as occurred in spontaneous activation, indicating that rubisco carbamylation is one facet of the rubisco activase reaction. The CO2 concentration required for one-half maximal rubisco activase activity was about 8 micromolar CO2. These observations are consistent with the postulated role of rubisco activase in regulating rubisco activity in vivo.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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