Purification and properties of ribulose 1,5-bisphosphate carboxylase from sunflower leaves
β Scribed by B. Ranty; G. Cavalie
- Publisher
- Springer-Verlag
- Year
- 1982
- Tongue
- English
- Weight
- 544 KB
- Volume
- 155
- Category
- Article
- ISSN
- 0032-0935
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π SIMILAR VOLUMES
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
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