Gene structure, expression in Escherichia coli and biochemical properties of the NAD+-dependent glyceraldehyde-3-phosphate dehydrogenase from Pinus sylvestris chloroplasts
Author:
Publisher
Elsevier BV
Subject
Genetics,General Medicine
Reference40 articles.
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2. Regulation of NADP-dependent glyceraldehyde-3-phosphate dehydrogenase activity in spinach chloroplasts;Baalmann;Bot. Acta,1994
3. 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
4. Backhausen, J.E., Vetter, S., Baalmann, E., Kitzmann, C., Scheibe, R., 1998. NAD+-dependent malate dehydrogenase and glyceraldehyde-3-phosphate dehydrogenase isoenzymes play an important role in dark metabolism of various plastid types. Planta ••, •••-••• (in press).
5. A rapid and sensitive method for the quantification of microgram quantities of protein using the principle of protein-dye binding;Bradford;Anal. Biochem.,1976
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