Renaturation of phosphorylase kinase activity from sodium dodecyl sulfate-polyacrylamide gels
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,Biochemistry,Biophysics
Reference22 articles.
1. Identification of the Ca2+-dependent modulator protein as the fourth subunit of rabbit skeletal muscle phosphorylase kinase
2. The Subunit Structure of Rabbit-Skeletal-Muscle Phosphorylase Kinase, and the Molecular Basis of Its Activation Reactions
3. Inhibition of the catalytic subunit of phosphorylase kinase by its alpha/beta subunits.
4. Homology of the .gamma. subunit of phosphorylase b kinase with cAMP-dependent protein kinase
5. High performance liquid chromatography purification and structural characterization of the subunits of rabbit muscle phosphorylase kinase.
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1. Physicochemical changes in phosphorylase kinase associated with its activation;Protein Science;2008-12
2. Self-association of the α Subunit of Phosphorylase Kinase as Determined by Two-hybrid Screening;Journal of Biological Chemistry;1999-12
3. Activators of Phosphorylase Kinase Alter the Cross-Linking of Its Catalytic Subunit to the C-Terminal One-Sixth of Its Regulatory α Subunit;Biochemistry;1999-02-01
4. The Detection of Enzyme Activity Following Sodium Dodecyl Sulfate–Polyacrylamide Gel Electrophoresis;Analytical Biochemistry;1998-06
5. Differential Affinity Cross-linking of Phosphorylase Kinase Conformers by the Geometric Isomers of Phenylenedimaleimide;Journal of Biological Chemistry;1997-10
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