Abstract:
:Mitochondrial citrate synthase was purified from leaves of Pisum sativum L. cv Progress 9. A three step purification was employed using ATP-Sepharose affinity chromatography which resulted in a 600-fold enrichment. Enzyme activity was assayed spectrophotometrically during greening of etiolated leaves under constant white light illumination. An increase (1.4 fold) in citrate synthase activity was observed in response to light. Immunoblot analysis of the same samples indicated a constant steady state level of citrate synthase on a per milligram protein basis. These investigations provide supportive evidence for the ability of this trichloroacetic acid cycle enzyme to be active in photosynthesizing tissue.
journal_name
Plant Physioljournal_title
Plant physiologyauthors
Unger EA,Vasconcelos ACdoi
10.1104/pp.89.3.719subject
Has Abstractpub_date
1989-03-01 00:00:00pages
719-23issue
3eissn
0032-0889issn
1532-2548journal_volume
89pub_type
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