TY  - JOUR
A1  - Meyer, Björn
A1  - Wittig, Ilka
A1  - Trifilieff, Elisabeth
A1  - Karas, Michael
A1  - Schägger, Hermann
T1  - Identification of two proteins associated with mammalian ATP synthase
T2  - Molecular & Cellular Proteomics
N2  - Bovine mitochondrial ATP synthase commonly is isolated as a monomeric complex that contains 16 protein subunits and the natural IF1 inhibitor protein in substoichiometric amounts. Alternatively ATP synthase can be isolated in dimeric and higher oligomeric states using digitonin for membrane solubilization and blue native or clear native electrophoresis for separation of the native mitochondrial complexes. Using blue native electrophoresis we could identify two ATP synthase-associated membrane proteins with masses smaller than 7 kDa and isoelectric points close to 10 that previously had been removed during purification. We show that in the mitochondrial membrane both proteins are almost quantitatively bound to ATP synthase. Both proteins had been identified earlier in a different context, but their association with ATP synthase was unknown. The first one had been named 6.8-kDa mitochondrial proteolipid because it can be isolated by chloroform/methanol extraction from mitochondrial membranes. The second one had been denoted as diabetes-associated protein in insulin-sensitive tissue (DAPIT), which may provide a clue for further functional and clinical investigations.
Y1  - 2021
UR  - http://publikationen.ub.uni-frankfurt.de/frontdoor/index/index/docId/76285
UR  - https://nbn-resolving.org/urn:nbn:de:hebis:30:3-762856
SN  - 1535-9476
VL  - 6
IS  - 10
SP  - 1690
EP  - 1699
PB  - American Society for Biochemistry and Molecular Biology Publications
CY  - Bethesda, Md
ER  -