Purification of a vanadate-sensitive ATPase from clathrin-coated vesicles of bovine brain.

  title={Purification of a vanadate-sensitive ATPase from clathrin-coated vesicles of bovine brain.},
  author={X. Sunney Xie and Dennis K. Stone and Efraim Racker},
  journal={The Journal of biological chemistry},
  volume={264 3},
Clathrin-coated vesicle acidification is mediated by an N-ethylmaleimide-sensitive, vanadate-resistant proton-translocating ATPase. This enzyme is a 530-kDa hetero-oligomer which catalyzes ATP-dependent proton pumping when reconstituted (Xie, X. S., and Stone, D. K. (1986) J. Biol. Chem. 261, 2492-2495). We now report the purification of a second ATPase from bovine brain clathrin-coated vesicles which is inhibited by both N-ethylmaleimide (1 mM) and vanadate (10 microM). Localization of the… Expand
Vanadate-sensitive ATPase from chromaffin granule membranes formed a phosphoenzyme intermediate and was activated by phosphatidylserine.
Results indicated that the vanadate-sensitive ATPase belongs to the P-type ATPases, which differ from known cation-translocating P- type ATPases. Expand
Membranes markers in highly purified clathrin-coated vesicles from Cucurbita hypocotyls
Highly purified cv fractions from zucchini hypocotyls cross-react with subunit antibodies from both vacuolar and PM H +-ATPases, and results are discussed in terms of recent findings on cv ATPases from bovine brain. Expand
Partial Purification and Characterization of the Vacuolar H+‐ATPase of Mammalian Synaptic Vesicles
Results strongly suggest that the abundant, multisubunit complex partially purified from brain synaptic vesicles by density gradient centrifugation is a vacuolar H+‐ATPase, essential for proton pumping as well as catecholamine uptake by mammalian synapticvesicles. Expand
Purification and Subunit Composition of a Cholinergic Synaptic Vesicle Glycoprotein, Phosphointermediate‐Forming ATPase
This composition suggests that the ATPase is a member of the P‐type, or phos‐phointermediate‐forming, family, but it was shown to be distinct from the ouabain‐sensitive Na+,K+‐ and Ca2+‐stimulated Mg2‐ATPases. Expand
Biochemical characterization of an electrogenic vacuolar proton pump in purified chicken osteoclast plasma membrane vesicles
  • P. Bekker, C. Gay
  • Chemistry, Medicine
  • Journal of bone and mineral research : the official journal of the American Society for Bone and Mineral Research
  • 1990
A well‐characterized chicken osteoclast plasma membrane vesicle preparation manifested Mg2+‐dependent ATP hydrolyzing activity and ATP, GTP, ITP, CTP, and ADP were all hydrolyzed effectively. Expand
Characterization of the P‐Type and V‐Type ATPases of Cholinergic Synaptic Vesicles and Coupling of Nucleotide Hydrolysis to Acetylcholine Transport
Both phosphointermediate‐ and vacuolar‐type ATPase activities found in cholinergic synaptic vesicles isolated from electric organ are immunoprecipitated by a monoclonal antibody to the SV2 epitope characteristic of synapticVesicles. Expand
ATPase activity of partially purified P-glycoprotein from multidrug-resistant Chinese hamster ovary cells.
A procedure for rapid partial purification of the protein in a highly active form and the ATPase activity could be distinguished from that of other ion-motive ATPases and membrane-associated phosphatases and is proposed to be directly attributable to P-glycoprotein. Expand
ATPases in Plant Coated Vesicles
Investigation ofractions containing highly purified clathrin coated vesicles from bovine brain and two plant sources finds immunological differences between the ATPases from animal and plant sources appear to exist. Expand
Identification and Functional Expression of Four Isoforms of ATPase II, the Putative Aminophospholipid Translocase
Four isoforms of ATPase II are identified in bovine brain by a combination of two major variations in their primary sequences and show that the structural variation of these isoforms has functional significance in both ATPase activity and phosholipid selectivity. Expand
Partial purification and characterization of the human erythrocyte Mg2+ ‐ATPase A candidate aminophospholipid translocase
A Mg2+‐ATPase‐enriched fraction was obtained from solubilized human erythrocyte membranes by ammonium sulphate precipitation and anion‐exchange chromatography and it is inferred that this enzyme is the same protein as the aminophospholipid translocase which regulates the membrane phospholipids transverse distribution in human ERYthrocytes by actively transporting aminophile from the outer to the inner monolayer. Expand