Co-purification of Pea and Bean Leaf Soluble Auxin-binding Proteins with Ribulose-1,5-Bisphosphate Carboxylase 1
AUTOR(ES)
Wardrop, Alison J.
RESUMO
Soluble auxin-binding proteins (ABPs) were purified to constant specific activity from bean and pea leaves by a procedure involving (NH4)2SO4 fractionation, anion exchange chromatography and gel filtration. Pea and bean ABPs exactly co-purify with ribulose-1,5-bisphosphate carboxylase (RuBPCase) in a variety of chromatographic separation procedures. The subunit compositions, electrophoretic purities and indole-3-acetic acid (IAA)-binding stoichiometries of the purified ABPs provide further evidence for the identity of RuBPCase and ABP. Pea ABP and bean ABP have dissociation constants for IAA of 0.8 and 1.3 micromolar, respectively, as determined by an (NH4)2SO4 precipitation assay for IAA-binding to insolubilized ABP. IAA can bind to soluble bean and pea ABP (RuBPCase) as determined by equilibrium dialysis with affinities and stoichiometries similar to those determined for insolubilized ABP.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=440541Documentos Relacionados
- Ligand Specificity of Bean Leaf Soluble Auxin-binding Protein 1
- Ribulose-1,5-bisphosphate carboxylase/oxygenase activase deficiency delays senescence of ribulose-1,5-bisphosphate carboxylase/oxygenase but progressively impairs its catalysis during tobacco leaf development.
- Bicarbonate Inhibits Ribulose-1,5-Bisphosphate Carboxylase
- Correlation of Carbonic Anhydrase and Ribulose-1,5-Bisphosphate Carboxylase/Oxygenase Expression in Pea.
- Effect of CO2 Concentration on Carbonic Anhydrase and Ribulose-1,5-Bisphosphate Carboxylase/Oxygenase Expression in Pea.
