Literature DB >> 17816743

Crystalline ribulose 1,5-bisphosphate carboxylase-oxygenase from spinach.

S Johal, D P Bourque.   

Abstract

Spinach fraction I protein (ribulose 1,5-bisphosphate carboxylase-oxy genase, E.C. 4.1.1.39) was crystallized on both an analytical and a preparative scale by vapor diffusion with polyethylene glycol (molecular weight, 6000) used as the precipitant. The identity of the crystalline material with fraction I protein was shown by gel electrophoresis in the presence of sodium dodecyl sulfate and immunological properties. The carboxylase and oxygenase activities copurify during crystallization, and the crystalline enzyme lacks copper and iron.

Entities:  

Year:  1979        PMID: 17816743     DOI: 10.1126/science.204.4388.75

Source DB:  PubMed          Journal:  Science        ISSN: 0036-8075            Impact factor:   47.728


  2 in total

1.  Effect of pH, Mg, CO(2) and Mercurials on the Circular Dichroism, Thermal Stability and Light Scattering of Ribulose 1,5-Bisphosphate Carboxylases from Alfalfa, Spinach and Tobacco.

Authors:  Y Tomimatsu; J W Donovan
Journal:  Plant Physiol       Date:  1981-10       Impact factor: 8.340

2.  Storage and maintaining activity of ribulose bisphosphate carboxylase/oxygenase.

Authors:  N P Hall; S D McCurry; N E Tolbert
Journal:  Plant Physiol       Date:  1981-06       Impact factor: 8.340

  2 in total

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