Purification and Assay of Rubisco Activase from Leaves

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Purification and assay of rubisco activase from leaves.

Ribulose 1,5-bisphosphate carboxylase/oxygenase (rubisco) activase protein was purified from spinach leaves by ammonium sulfate precipitation and ion exchange fast protein liquid chromatography. This resulted in 48-fold purification with 70% recovery of activity and yielded up to 18 milligrams of rubisco activase protein from 100 grams of leaves. Based on these figures, the protein comprised ap...

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Purification and species distribution of rubisco activase.

Ribulose-1,5-bisphosphate carboxylase/oxygenase (rubisco) activase, a soluble chloroplast protein which promotes light-dependent rubisco activation, was partially purified from spinach chloroplasts by ion-exchange and gel-filtration fast protein liquid chromatography. The protein could also be isolated using rate zonal centrifugation in sucrose gradients followed by conventional ion-exchange on...

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Rubisco, Rubisco activase, and global climate change.

Global warming and the rise in atmospheric CO(2) will increase the operating temperature of leaves in coming decades, often well above the thermal optimum for photosynthesis. Presently, there is controversy over the limiting processes controlling photosynthesis at elevated temperature. Leading models propose that the reduction in photosynthesis at elevated temperature is a function of either de...

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Rubisco activase constrains the photosynthetic potential of leaves at high temperature and CO2.

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ژورنال

عنوان ژورنال: Plant Physiology

سال: 1988

ISSN: 0032-0889,1532-2548

DOI: 10.1104/pp.88.4.1008