Isolation and Some Properties of Ribulose-1, 5-Bisphosphate Carboxylase-Oxygenase from Red Kidney Bean Primary Leaves 1
AUTOR(ES)
Harris, Gary C.
RESUMO
Purification of ribulose-1,5-bisphosphate carboxylase from primary leaves of Phaseolus vulgaris var. Red Kidney with ammonium sulfate precipitation, ion exchange chromatography, and gel filtration resulted in the complete loss of detectable oxygenase activity and the retention of a low velocity and a high Km form of both the carboxylase and oxygenase. The polyethylene glycol-6000-purified ribulose-1, 5-bisphosphate oxygenase displayed a broad pH optimum (7.9-9.4) and a high Km for O2 and ribulose 1,5-bisphosphate (0.90 mm and 0.25 mm, respectively). Initiation of the oxygenase reaction with protein rather than ribulose 1,5-bisphosphate resulted in reduced activity. The enzymes prepared by the two purification procedures were electrophoretically different.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=542697Documentos Relacionados
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