Identification of the highly reactive sulfhydryl group of pig kidney fructose 1,6-bisphosphatase at cysteine 128.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference28 articles.
1. Amino acid sequence of the COOH-terminal region of fructose-1,6-bisphosphatases in relation to cyclic AMP-dependent phosphorylation.
2. Bovine hepatic fructose 1,6-diphosphatase: Modification of the catalytic and allosteric properties by sulfhydryl reagents
3. Regulatory sulfhydryl groups, conformational change, and allosteric inhibition in rabbit muscle fructose diphosphatase
4. The Effect of pH on the Kinetics of Beef-Liver Fructose Bisphosphatase
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1. Reactivity of bromide for radiolabeling of proteins and peptides;Applied Radiation and Isotopes;1997-07
2. Modification of cys-128 of pig kidney fructose 1,6-bisphosphatase with different thiol reagents: Size dependent effect on the substrate and fructose-2,6-bisphosphate interaction;Journal of Protein Chemistry;1993-04
3. Evidence for heat-stable liver cytosol substance(s) capable of causing oxidative activation of fructose 1,6-bisphosphatase;Biochemical and Biophysical Research Communications;1992-01
4. Structure refinement of fructose-1,6-bisphosphatase and its fructose 2,6-bisphosphate complex at 2.8 Å resolution;Journal of Molecular Biology;1990-04
5. Inactivation of fructose-1,6-bisphosphatase by o -phthalaldehyde;Biochemical and Biophysical Research Communications;1988-02
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