The state of activation of ribulose-1,5-bisphosphate carboxylase in wheat leaves
โ Scribed by F. A. Boyle; A. J. Keys
- Publisher
- Springer
- Year
- 1987
- Tongue
- English
- Weight
- 615 KB
- Volume
- 11
- Category
- Article
- ISSN
- 0166-8595
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โฆ Synopsis
In light and in darkness, exposure of leaf segments to CO~-free atmospheres caused a marked reduction in extractable RuBP carboxylase activity, By contrast, darkness caused a relatively small decrease in carboxylase activity in extracts from leaf segments kept in air containing CO 2 . Recovery of carboxylase activity in leaves during illumination in air after exposure to CO 2 -free conditions paralleled recovery of capacity for photosynthesis; in darkness recovery of carboxylase activity in leaves was slower than in the light. Extracts from leaves exposed to CO 2 -free conditions recovered activity when provided with CO s and Mg2รท; there were clearly, however, substances in the extracts that modified the activity achieved and caused anomalous decreases and increases with time after extraction. Studies of the effect of orthophosphate on the activity of purified wheat carboxylase in vitro were consistent with the view that many of the effects observed on the activity of crude leaf extracts were due to orthophosphate content.
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In crude extracts from the primary leaf of wheat seedlings, Triticum aestivum L., cv. Olympic, maximum proteinase activity, as determined by measuring the rate of release of amino nitrogen from ribulose-bisphosphate carboxylase (RuBPCase), was found to be obtained only when EDTA and L-cysteine were
Mutagenesis in vitro of the gene encoding the large subunit of ribulose-1,5-bisphosphate carboxylase/ oxygenase (EC 4.1.1.39) from Anacystis nidulans was used to generate novel enzymes. Two conserved residues, threonine 4 and lysine 11 in the N-terminus were changed. The substitution of threonine 4
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