Purification and characterization of mitochondrial citrate synthase.

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 Physiol

journal_title

Plant physiology

authors

Unger EA,Vasconcelos AC

doi

10.1104/pp.89.3.719

subject

Has Abstract

pub_date

1989-03-01 00:00:00

pages

719-23

issue

3

eissn

0032-0889

issn

1532-2548

journal_volume

89

pub_type

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