Functional studies of chloroplast glyceraldehyde-3-phosphate dehydrogenase subunits A and B expressed in Escherichia coli: Formation of highly active A4 and B4 homotetramers and evidence that aggregation of the B4 complex is mediated by the B subunit carboxy terminus

Plant Molecular Biology

Volumn 32, Issue 3, 1996, Pages 505-513

  Baalmann, Elisabeth ^a   Scheibe, Renate ^a   Cerff, Rüdiger ^b   Martin, William ^b  

^a UNIVERSITY OF OSNABRÜCK   (Germany)

^b TECHNICAL UNIVERSITY OF BRAUNSCHWEIG   (Germany)

Author keywords

Enzyme activation; Enzyme structure; Glyceraldehyde 3 phosphate dehydrogenase; Light regulation; Redox

Indexed keywords

COMPLEMENTARY DNA; GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE; HYBRID PROTEIN; PLANT DNA;

AMINO ACID SEQUENCE; ARTICLE; CHEMISTRY; CHLOROPLAST; ENZYMOLOGY; ESCHERICHIA COLI; GENETICS; ISOLATION AND PURIFICATION; MOLECULAR GENETICS; MOLECULAR WEIGHT; NUCLEOTIDE SEQUENCE; PROTEIN CONFORMATION; SPINACH;

AMINO ACID SEQUENCE; BASE SEQUENCE; CHLOROPLASTS; DNA, COMPLEMENTARY; DNA, PLANT; ESCHERICHIA COLI; GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASES; MOLECULAR SEQUENCE DATA; MOLECULAR WEIGHT; PROTEIN CONFORMATION; RECOMBINANT FUSION PROTEINS; SPINACIA OLERACEA;

EID: 0030293673     PISSN: 01674412     EISSN: None     Source Type: Journal    
DOI: 10.1007/BF00019102     Document Type: Article

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