The halobacterial H+-translocating ATP synthase relates to the eukaryotic anion-sensitive H+-ATPase.
The H+-translocating ATP synthase of Halobacterium halobium (Y. Mukohata and M. Yoshida (1987) J. Biochem. 102, 797-802) includes a catalytic moiety of 320 kDa which is isolated as an azide-insensitive ATPase (T. Nanba and Y. Mukohata (1987) J. Biochem. 102, 591-598). The polyclonal antibody against this archaebacterial ATPase cross-reacts with the anion-sensitive H+-ATPase of red beet, Beta vulgaris, tonoplast as well as with another archaebacterial ATPase from Sulfolobus acidocaldarius. The affinity is much higher than to F1-ATPase from spinach chloroplasts or to Ca2+-ATPase from sarcoplasmic reticulum of rabbit skeletal muscle.
D001105:Archaea / Q000201:enzymology; D002462:Cell Membrane / Q000201:enzymology; D002477:Cells / Q000201:enzymology*; D005057:Eukaryotic Cells / Q000201:enzymology*; D006217:Halobacterium / Q000201:enzymology*; D046911:Macromolecular Substances; D008970:Molecular Weight; D006180:Proton-Translocating ATPases / Q000378:metabolism*
D046911:Macromolecular Substances; D006180:Proton-Translocating ATPases