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
Depression of the synthesis of the intermediate and large forms of ribulose-1,5-bisphosphate carboxylase/oxygenase inRhodopseudomonas capsulata
โ Scribed by Jessup M. Shively; Edgar Davidson; Barry L. Marrs
- Publisher
- Springer
- Year
- 1984
- Tongue
- English
- Weight
- 541 KB
- Volume
- 138
- Category
- Article
- ISSN
- 0302-8933
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โฆ Synopsis
Rhodopseudomonas capsulata produces both an intermediate (I) and a large (L) form of ribulose-l,5-bisphosphate carboxylase/oxygenase. Both forms are derepressed under CO2-1imiting conditions. The L-form of the enzyme is completely repressed when the culture is grown either photoautotrophically or photoheterotrophically with malate as the electron donor. The L-form is derepressed in the late logarithmic phase of growth when cells are grown photoheterotrophically with butyrate as the electron donor and the NaHCO3 supplement is 0.01%. The level of the I-form is increased about fivefold under latter growth conditions when compared to malate-grown cells. Analytical ultracentrifugation revealed the molecular masses of the Iand L-forms to be 300,000 and 542,000, respectively. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis showed the I-form to be composed of only one type subunit with a molecular weight of 64,000. The L-form possessed both large and small subunits with molecular weights of 58,000 and I0,000.
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