[HTML][HTML] Identification and characterization of a novel 9.2-kDa membrane sector-associated protein of vacuolar proton-ATPase from chromaffin granules
J Ludwig, S Kerscher, U Brandt, K Pfeiffer… - Journal of Biological …, 1998 - ASBMB
Vacuolar proton-translocating ATPase (holoATPase and free membrane sector) was
isolated from bovine chromaffin granules by blue native polyacrylamide gel electrophoresis.
A 5-fold excess of membrane sector over holoenzyme was determined in isolated chromaffin
granule membranes. M9. 2, a novel extremely hydrophobic 9.2-kDa protein comprising 80
amino acids, was detected in the membrane sector. It shows sequence and structural
similarity to Vma21p, a yeast protein required for assembly of vacuolar ATPase. A second …
isolated from bovine chromaffin granules by blue native polyacrylamide gel electrophoresis.
A 5-fold excess of membrane sector over holoenzyme was determined in isolated chromaffin
granule membranes. M9. 2, a novel extremely hydrophobic 9.2-kDa protein comprising 80
amino acids, was detected in the membrane sector. It shows sequence and structural
similarity to Vma21p, a yeast protein required for assembly of vacuolar ATPase. A second …