Modification of lysine 501 in Na,K-ATPase reveals coupling between cation occupancy and changes in the ATP binding domain

Keyphrases

• K-ATPase 100%
• Lysine 100%
• ATP-binding Domain 100%
• Cation Occupancy 100%
• Sodium 40%
• Potassium 40%
• Bound Form 40%
• Sodium Pump 40%
• Canine 20%
• Reversed-phase HPLC 20%
• Amino Acid Sequence 20%
• Enzymatic Activity 20%
• ATP Synthase 20%
• Imidazole 20%
• High-affinity Binding 20%
• Nucleotide-binding Domain 20%
• Differential Effects 20%
• Nitro 20%
• Conformational Transition 20%
• Irreversible Loss 20%
• Spatial Organization 20%
• Potassium Ion 20%
• Trypsin Treatment 20%
• Low-affinity Binding Sites 20%
• Sodium Ion 20%

Biochemistry, Genetics and Molecular Biology

• Binding Domain 100%
• ATPase 100%
• Adenosine Triphosphate 100%
• Lysine 100%
• Enzyme 60%
• Conformation 40%
• Enzyme Activity 20%
• Binding Affinity 20%
• Reverse Phase High Performance Liquid Chromatography 20%
• Protein Sequencing 20%
• Conformational Change 20%

Neuroscience

• Adenosine Triphosphatase (Potassium Sodium) 100%
• Adenosine Triphosphate 100%
• Lysine 100%
• Binding Affinity 20%
• Protein Sequencing 20%
• Enzyme Activity 20%
• Adenosine Triphosphatase 20%
• Imidazole 20%