A rapid and novel method for purification of 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/17/1-3/269/19391874/17-1-3-269.pdf
Reference13 articles.
1. Ribulose-1, 5-diphosphate carboxylase of Chromatium strain D1
2. Structure and function of chloroplast proteins. XVI. Ribulose 1,5-diphosphate carboxylase from Chromatium strain D
3. Catalytic role of subunit A in ribulose-1,5-diphosphate carboxylase from Chromatium strain D
4. Structure and function of chloroplast proteins. XXVI. Subunit structure of Chromatium ribulose-1,5-bisphosphate carboxylase
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1. In SituMeasurements of Ribulose-1,5-bisphosphate Carboxylase Activity by Nuclear Magnetic Resonance;Analytical Biochemistry;1998-03
2. Purification and characterization of the thermostable ribulose-1,5-bisphosphate carboxylase/oxygenase from the thermophilic purple bacterium Chromatium tepidum;European Journal of Biochemistry;1989-09
3. Isolation of L8 and L8S8 forms of ribulose bisphosphate carboxylase/oxygenase from Chromatium vinosum;Archives of Microbiology;1985-06
4. Subunit dissociation and reconstitution of ribulose-1,5-bisphosphate carboxylase from Chromatium vinosum;Archives of Biochemistry and Biophysics;1985-02
5. The Major Protein of Chloroplast Stroma, Ribulosebisphosphate Carboxylase;Cell Components;1985
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