Ribulose-1,5-bisphosphate carboxylase-oxygenase: Aspects and prospects
✍ Scribed by Günter F. Wildner
- Book ID
- 110897891
- Publisher
- John Wiley and Sons
- Year
- 1981
- Tongue
- English
- Weight
- 518 KB
- Volume
- 52
- Category
- Article
- ISSN
- 0031-9317
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The structure of spinach ribulose 1,5-bisphosphate carboxylase/oxygenase (EC 4.1.1.39) has been investigated by tilted-view electron microscopy of negatively stained monolayer crystals and image processing. The structure determined consists of a cylinder of octagonal cross-section with a large centr
The substrate specificity factor, VcKo/ V o Kc, of spinach (Spinacia oleracea L.) ribulose 1,5-bisphosphate carboxylase/oxygenase was determined at ribulosebisphosphate concentrations between 0.63 and 200 gM, at pH values between 7.4 and 8.9, and at temperatures in the range of 5 ~ C to 40 ~ C. The
Ribulose 1,5-bisphosphate carboxylase (EC.4.1.1.39) has been obtained from Nicotiana tabacum leaf homogenates with specific activites from 0.5 to 0.8 µmol CO2 fixed (mg protein min)(-1). These activities are reconciled with much lower, previously reported activities. The results suggest that if the