An improved purification protocol for ribulose 1,5-bisphosphate carboxylase fromChromatium vinosum
Author:
Publisher
Oxford University Press (OUP)
Subject
Genetics,Molecular Biology,Microbiology
Link
http://academic.oup.com/femsle/article-pdf/12/2/105/19077253/12-2-105.pdf
Reference13 articles.
1. Structure and function of chloroplast proteins. XVI. Ribulose 1,5-diphosphate carboxylase from Chromatium strain D
2. Catalytic role of subunit A in ribulose-1,5-diphosphate carboxylase from Chromatium strain D
3. Structure and function of chloroplast proteins. XXVI. Subunit structure of Chromatium ribulose-1,5-bisphosphate carboxylase
4. Ribulose Diphosphate Carboxylase in Thiorhodaceae
5. Light-dependent utilization of organic compounds and photoproduction of molecular hydrogen by photosynthetic bacteria; relationships with nitrogen metabolism
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1. In SituMeasurements of Ribulose-1,5-bisphosphate Carboxylase Activity by Nuclear Magnetic Resonance;Analytical Biochemistry;1998-03
2. Anoxygenic Phototrophic Bacteria: Physiology and Advances in Hydrogen Production Technology;Advances in Applied Microbiology;1993
3. Sequence and expression of genes encoding the large and small subunits of ribulose 1,5-bisphosphate carboxylase/oxygenase from Chromatium vinosum;Gene;1991-01
4. Distinct properties of Escherichia coli products of plant-type ribulose-1,5-bisphosphate carboxylase/oxygenase directed by two sets of genes from the photosynthetic bacterium Chromatium vinosum.;Journal of Biological Chemistry;1990-10
5. Expressed genes for plant-type ribulose 1,5-bisphosphate carboxylase/oxygenase in the photosynthetic bacterium Chromatium vinosum, which possesses two complete sets of the genes;Journal of Bacteriology;1989-05
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