pH dependence of the reverse reaction catalyzed by phosphofructokinase I from Escherichia coli : Implications for the role of Asp 127
Author:
Funder
CNRS
Universitkc Paris
Publisher
Wiley
Subject
Molecular Biology,Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1002/pro.5560010207/fullpdf
Reference11 articles.
1. Kinetics of the allosteric interactions of phosphofructokinase from Escherichia coli;Blangy;J. Mol. Biol.,1968
2. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of proteindye binding;Bradford;Anal. Biochem.,1976
3. pH dependence of the kinetic properties of allosteric phosphofructokinase from Escherichia coli;Deville-Bonne;Biochemistry,1991
4. Ordered disruption of subunit interfaces during the stepwise reversible dissociation of Escherichia coli phosphofructokinase with KSCN;Deville-Bonne;Biochemistry,1989
5. Buffers of constant ionic strength for studying pH-dependent processes;Ellis;Methods Enzymol.,1982
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