Purification and properties of a vanadate- and N-ethylmaleimide-sensitive ATPase from chromaffin granule membranes

Medicine & Life Sciences

• N-Ethylmaleimide-Sensitive Proteins 100%
• Chromaffin Granules 98%
• Vanadates 81%
• Adenosine Triphosphatases 44%
• Membranes 37%
• Ethylmaleimide 35%
• Adenosine Triphosphate 34%
• Enzymes 34%
• Peptides 22%
• Lighting 19%
• vanadate-sensitive ATPase 17%
• 2'-deoxyadenosine triphosphate 16%
• Sch 28080 16%
• Ions 14%
• H(+)-K(+)-Exchanging ATPase 14%
• Dicyclohexylcarbodiimide 14%
• Monovalent Cations 12%
• Proton-Translocating ATPases 11%
• Omeprazole 10%
• Ouabain 10%
• sodium-translocating ATPase 9%
• Anions 9%
• Guanosine Triphosphate 9%
• Organelles 8%
• Binding Sites 6%
• Proteins 3%

Chemical Compounds

• N-Ethylmaleimide 45%
• Purification 42%
• Polypeptide 41%
• Illumination 22%
• Monovalent Anion 17%
• Omeprazole 17%
• Ouabain 15%
• Monoatomic Monocation 14%
• Molecular Mass 11%
• Ion 9%
• Protein 5%