Pea chloroplast glutathione reductase: purification and characterization. Academic Article

abstract

• Glutathione reductase (EC 1.6.4.2) was purified from intact pea (Pisum sativum) chloroplasts by a method which includes affinity chromatography on ADP-agarose. Fractions from the affinity column which had glutathione reductase activity consisted of polypeptides of 60 and 32 kilodaltons. Separation of the proteins by electrophoresis on native gels showed that glutathione reductase activity was associated with 60 kilodalton polypeptides and not with the 32 kilodalton polypeptides. Antibodies to spinach whole leaf glutathione reductase (60 kilodaltons) cross-react with the chloroplast 60 kilodalton glutathione reductase but not the 32 kilodalton polypeptides. In the absence of dithiothreitol the 60 kilodalton polypeptides showed a shift in apparent molecular weight on sodium dodecyl sulfate gels to 72 kilodaltons. Dithiothreitol did not alter the activity of the chloroplast enzyme. Chloroplast glutathione reductase is relatively insensitive to NADPH.

authors

• Mullet, John

published proceedings

• Plant Physiol

author list (cited authors)

• Connell, J. P., & Mullet, J. E.

citation count

• 66

complete list of authors

• Connell, JP||Mullet, JE

publication date

• October 1986

publisher

• Oxford University Press (OUP)  Publisher

published in

• PLANT PHYSIOLOGY  Journal

keywords

• 0601 Biochemistry And Cell Biology

PubMed Central ID

• 16665034

Digital Object Identifier (DOI)

• 10.1104/pp.82.2.351

start page

• 351

end page

• 356

volume

• 82

issue

• 2

URL

• http://dx.doi.org/10.1104/pp.82.2.351