Ribulose 1,5-bisphosphate (RuBP) carboxylase (EC 4.1.1.39) activity was approximately equally distributed between supernatant and pellet fractions produced by differential centrifugation of disrupted cells of Chlorogloeopsis fritschii. Low ionic strength buffer favoured the recovery of particulate R
d-Ribulose 1,5-bisphosphate carboxylase and polyhedral inclusion bodies inNitrosomonas spec
โ Scribed by Heinz Harms; Hans-Peter Koops; Heike Martiny; Michael Wullenweber
- Publisher
- Springer
- Year
- 1981
- Tongue
- English
- Weight
- 296 KB
- Volume
- 128
- Category
- Article
- ISSN
- 0302-8933
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โฆ Synopsis
Polyhedral inclusion bodies were isolated from exponentially grown cells of Nitrosomonas spec. The bodies contained D-ribulose 1,5-bisphosphate carboxylase. The specific activity of the enzyme was 0.0122 pmol COz fixed per min per mg of protein.
๐ SIMILAR VOLUMES
The data on the primary structure of ribulose-1,5-bisphosphate carboxylase/oxygenase are reviewed. Examples of their use as markers and in the elucidation of the evolution, adaptation and function of this key enzyme are given.
Improved methods for the activation and assay of D-ribulose-1,5-bisphosphate carboxylase and oxygenase are described. The importance of fully activating the enzyme before starting either reaction is emphasized. The enzyme is activated by preincubation with 20 mM M&l, and 10 mM NaHCO,, pH 8.6. To avo