| First Author | Ludwig J | Year | 1998 |
| Journal | J Biol Chem | Volume | 273 |
| Issue | 18 | Pages | 10939-47 |
| PubMed ID | 9556572 | Mgi Jnum | J:47435 |
| Mgi Id | MGI:1203438 | Doi | 10.1074/jbc.273.18.10939 |
| Citation | Ludwig J, et al. (1998) Identification and characterization of a novel 9.2-kDa membrane sector-associated protein of vacuolar proton-ATPase from chromaffin granules. J Biol Chem 273(18):10939-47 |
| abstractText | 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 membrane sector-associated protein (M8-9) was identified and characterized by amino-terminal protein sequencing. |
