Open AccessAffinity chromatography, on fructose‐bisphosphatase–Sepharose, of two chloroplastic thioredoxins F
Author(s) -
BUC Jean,
RIVIÈRE Mireille,
GONTERO Brigitte,
SAUVE Paul,
MEUNIER JeanClaude,
RICARD Jacques
Publication year - 1984
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1984.tb08086.x
Subject(s) - fructose 1,6 bisphosphatase , affinity chromatography , thioredoxin , biochemistry , sepharose , chemistry , chromatography , dimer , fructose , ultracentrifuge , ionic strength , enzyme , organic chemistry , aqueous solution
A new method of purification of chloroplastic thioredoxins has been presented. This method is based on affinity chromatography on fructose‐bisphosphatase—Sepharose columns. Two thioredoxin, f A and f B , may be extracted and purified to homogeneity from the same leaf extract. Whereas f A is monomeric and has an M r of 11400 ± 500, f B is dimeric with an M r of 18000 ± 600. The dimer dissociates in two halves in the ultracentrifuge under the effect of high pressures. Raising the ionic strength results in the same effect. Thioredoxins f A and f B activate to similar extents chloroplastic fructose bisphosphatase and NADP–malate dehydrogenase. Chloroplastic sedoheptulose bisphosphatase is activated by thioredoxin f B but not by thioredoxin f A .