Pyruvate Dehydrogenase Complex from Higher Plant Mitochondria and Proplastids 1
AUTOR(ES)
Reid, E. Ellen
RESUMO
The pyruvate dehydrogenase complex from pea (Pisum sativum L.) mitochondria was purified 23-fold by high speed centrifugation and glycerol gradient fractionation. The complex had a s20,w of 47.5S but this is a minimal value since the complex is unstable. The complex is specific for NAD+ and pyruvate; NADP+ and other keto acids give no reaction. Mg2+, thiamine pyrophosphate, and cysteine are also required for maximal activity. The pH optimum for the complex was between 6.5 and 7.5.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=543307Documentos Relacionados
- Pyruvate Dehydrogenase Complex from Higher Plant Mitochondria and Proplastids: Kinetics 1
- Pyruvate Dehydrogenase Complex from Higher Plant Mitochondria and Proplastids: Regulation 1
- Regulation of Steady State Pyruvate Dehydrogenase Complex Activity in Plant Mitochondria 1: Reactivation Constraints
- Regulation of Plant Pyruvate Dehydrogenase Complex by Phosphorylation 1
- Plant Pyruvate Dehydrogenase Complex: II. ATP-Dependent Inactivation and Phosphorylation 1
