Ludwig J, Kerscher S, Brandt U, Pfeiffer K, Getlawi F, Apps D K, Schägger H
Zentrum der Biologischen Chemie, Universitätsklinikum Frankfurt, D-60590 Frankfurt, Germany.
J Biol Chem. 1998 May 1;273(18):10939-47. doi: 10.1074/jbc.273.18.10939.
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.
通过蓝色天然聚丙烯酰胺凝胶电泳从牛嗜铬颗粒中分离出液泡质子转运ATP酶（全酶和游离膜结构域）。在分离的嗜铬颗粒膜中，测定膜结构域相对于全酶过量5倍。在膜结构域中检测到一种新型的疏水性极强的9.2 kDa蛋白质M9.2，它由80个氨基酸组成。它与液泡ATP酶组装所需的酵母蛋白Vma21p具有序列和结构相似性。通过氨基末端蛋白质测序鉴定并表征了第二种与膜结构域相关的蛋白质（M8-9）。
