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 ca
Location of chromosomal control of ribulose bisphosphate carboxylase amounts in wheat
โ Scribed by Jellings, Anita J. ;Leese, Brenda M. ;Leech, Rachel M.
- Publisher
- Springer
- Year
- 1983
- Tongue
- English
- Weight
- 290 KB
- Volume
- 192
- Category
- Article
- ISSN
- 0026-8925
No coin nor oath required. For personal study only.
๐ SIMILAR VOLUMES
Complete stoichiometry of the reaction catalyzed by ribulose l$bisphosphate (RuBP) oxygenase from spinach and Rhodospirillum rubrum has been determined. Before initiation and after termination, RuBP has been measured either by release of equimolar orthophosphate at 25'C in the presence of 1 N NaOH o
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
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