Nucleotide binding sites and chemical modification of the chromaffin granule proton ATPase.

Keyphrases

• Chemical Modification 100%
• N-ethylmaleimide 100%
• Nucleotide Binding Site 100%
• Chromaffin Granules 100%
• Proton ATPase 100%
• Mg2+ 66%
• Purified Enzymes 66%
• Micromolar Concentration 66%
• Ca2+ 33%
• ATP Synthase 33%
• Polypeptide 33%
• Nitrate 33%
• Highly Active 33%
• I to 33%
• Chloro 33%
• Mn2+ 33%
• Co2+ 33%
• Zn2+ 33%
• Diazole 33%
• Pumping Activity 33%
• Divalent Cations 33%
• Proton Pumping 33%
• Azido 33%
• Allosteric Enzyme 33%
• Proton Pump 33%
• Saturation Curve 33%
• Thiocyanate 33%
• Mg2+ Binding 33%

Pharmacology, Toxicology and Pharmaceutical Science

• Binding Site 100%
• Adenosine Triphosphate 100%
• Proton Transporting Adenosine Triphosphatase 100%
• Phosphorus 32 50%
• Magnesium Ion 50%
• N Ethylmaleimide 50%
• Adenosine Diphosphate 33%
• Proton Pump 33%
• Adenosine Triphosphatase 16%
• Polypeptide 16%
• Calcium Ion 16%
• Imidazole 16%
• Divalent Cation 16%
• Sulfur 35 16%
• Zinc Ion 16%
• Thiocyanate 16%
• Sulfate 16%