Pisum sativum mitochondrial pyruvate dehydrogenase can be assembled as a functional α2β2 heterotetramer in the cytoplasm of Pichia pastoris

Protein Expression and Purification

Volumn 19, Issue 2, 2000, Pages 276-283

  Moreno, J Ignacio ^a   David, Nancy R ^a   Miernyk, Jan A ^a,b   Randall, Douglas D ^a  

^a University of Missouri   (United States)

^b AGRICULTURAL RESEARCH SERVICE   (United States)

Author keywords

Assembly; Mitochondrial; Phosphorylation; Pyruvate dehydrogenase; Yeast

Indexed keywords

CHROMATOGRAPHY; CYTOPLASM; DECARBOXYLATION; ENZYME ACTIVITY; ENZYME PURIFICATION; ENZYME SUBUNIT; ENZYME SYNTHESIS; GEL PERMEATION CHROMATOGRAPHY; MAGNESIUM; MITOCHONDRION; POTASSIUM FERRICYANIDE; PROTEIN ASSEMBLY; PROTEIN PHOSPHORYLATION; PYRUVATE DEHYDROGENASE; RECOMBINANT ENZYME; THIAMIN PYROPHOSPHATE;

PICHIA PASTORIS; PISUM SATIVUM; SATIVUM;

EID: 0033948711     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1006/prep.2000.1247     Document Type: Article

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