Thermodynamic Linkages in Rabbit Muscle Pyruvate Kinase: Kinetic, Equilibrium, and Structural Studies

Keyphrases

• Allosteric Inhibitor 10%
• Allosteric Regulation 10%
• Association Constant 10%
• Binding Constant 10%
• Binding Site 10%
• Binding Studies 10%
• Conformational Change 10%
• Cooperativity 10%
• Equilibrium Binding 20%
• Equilibrium Experiments 10%
• Hydrodynamic Properties 10%
• Kinetic Equilibrium 100%
• Kinetic Measurements 10%
• Ligand Effects 10%
• Loosening 10%
• Monod-Wyman-Changeux Model 10%
• Phenylalanine 100%
• Phosphoenolpyruvate 30%
• Protein Structure 10%
• Pyruvate Kinase 100%
• Rabbit muscle 100%
• Regulatory Behavior 10%
• Sedimentation Coefficient 10%
• Sedimentation Equilibrium 10%
• Sedimentation Velocity 10%
• Sedimentation Velocity Experiments 10%
• Steady-state Kinetics 20%
• Sulfhydryl 10%
• Thermodynamic Linkage 100%
• Two-state Model 10%
• Velocity Sedimentation 10%

Biochemistry, Genetics and Molecular Biology

• Allosteric Regulation 10%
• Binding Affinity 10%
• Binding Site 10%
• Binding Study 10%
• Conformational Change 10%
• Cooperation 10%
• Enzyme 20%
• Gene Linkage 100%
• Leporidae 100%
• Phenylalanine 100%
• Protein Structure 10%
• Pyruvate Kinase 100%
• Sedimentation Equilibrium 10%
• Sedimentation Rate 30%
• Steady State 20%

Immunology and Microbiology

• Allosterism 10%
• Binding Affinity 10%
• Binding Site 10%
• Conformational Transition 10%
• Leporidae 100%
• Muscle 100%
• Phenylalanine 100%
• Protein Structure 10%
• Sedimentation Rate 30%
• Steady State 20%