TY  - JOUR
A1  - Ludwig, Jürgen
A1  - Kerscher, Stefan
A1  - Brandt, Ulrich
A1  - Pfeiffer, Kathy
A1  - Getlawi, Fariha
A1  - Apps, David K.
A1  - Schägger, Hermann
T1  - Identification and characterization of a novel 9.2-kDa membrane sector-associated protein of vacuolar proton-ATPase from chromaffin granules
T2  - Journal of biological chemistry
N2  - 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.
Y1  - 2021
UR  - http://publikationen.ub.uni-frankfurt.de/frontdoor/index/index/docId/75870
UR  - https://nbn-resolving.org/urn:nbn:de:hebis:30:3-758705
SN  - 0021-9258
VL  - 273.1998
IS  - 18
SP  - 10939
EP  - 10947
PB  - American Society for Biochemistry and Molecular Biology Publications
CY  - Bethesda, Md
ER  -