Results 1 to 10 of about 5,086 (127)
Regulation of proton-translocating V-ATPases [PDF]
Journal of Experimental Biology, 1997 ABSTRACT Vacuolar-type ATPases (V-ATPases) are proton-translocating enzymes that occur in the endomembranes of all eukaryotes and in the plasma membranes of many eukaryotes. They are multisubunit, heteromeric proteins composed of two structural domains, a peripheral, catalytic V1 domain and a membrane-spanning Vo domain.
H, Merzendorfer +4 more
openaire +2 more sources
Localization of a Proton-Translocating ATPase on Sucrose Gradients [PDF]
Plant Physiology, 1982 Ionophore-stimulated ATPase activity and ATP-dependent quinacrine quench were enriched in parallel when microsomal vesicles were prepared from corn (Crow Single Cross Hybrid WF9-Mo17) roots and collected on a cushion of 10% dextran. Activities were highest in the apical 1.5 centimeters of the roots.
F M, Dupont +2 more
openaire +2 more sources
Electrogenic Proton Translocation by the ATPase of Sugarcane Vacuoles [PDF]
Plant Physiology, 1985 Existence of a proton-translocating ATPase on the tonoplast of higher plants has been further confirmed by use of two experimental systems: (a) intact isolated vacuoles from sugarcane cells and (b) vesicles prepared from the same source. Addition of MgATP to vacuoles polarized the tonoplast by 40 millivolts to a value of +20 millivolts, but a large ...
M, Thom, E, Komor
openaire +2 more sources
The role of the host—Neutrophil biology
Periodontology 2000, EarlyView., 2023 Abstract Neutrophilic polymorphonuclear leukocytes (neutrophils) are myeloid cells packed with lysosomal granules (hence also called granulocytes) that contain a formidable antimicrobial arsenal. They are terminally differentiated cells that play a critical role in acute and chronic inflammation, as well as in the resolution of inflammation and wound ...
Iain L. C. Chapple +4 more
wiley +1 more source
Fluoride inhibition of proton-translocating ATPases of oral bacteria [PDF]
Infection and Immunity, 1987 The ATPases of isolated membranes of lactic acid bacteria were found to be inhibited by fluoride in a complex manner. Among the enzymes tested, that of Streptococcus mutans GS-5 was the most sensitive to fluoride, and the initial rate of hydrolysis of ATP was reduced 50% by approximately 3 mM fluoride.
S V, Sutton, G R, Bender, R E, Marquis
openaire +2 more sources
Proton translocation induced by ATPase activity in chloroplasts [PDF]
FEBS Letters, 1970 Proton uptake by chloroplasts was induced by light‐triggered ATPase activity. A quotient of two was obtained when the initial rate of proton uptake was divided by the rate of Pi released from ATP. Gramicidin accelerated the rate of ATPase activity and reduced the H+/Pi ratio to 1.4. The results were found to be consistent with the chemiosmotic theory.
openaire +2 more sources
The assignment of the Ca2+‐ATPase activity of chromaffin granules to the proton translocating ATPase [PDF]
FEBS Letters, 1985 Ca2+‐ATPase H+‐ATPase Proton pump Chromaffin granule Adrenal medulla
Flatmark, Torgeir +3 more
openaire +2 more sources
Proton translocation driven by ATP hydrolysis in V‐ATPases
FEBS Letters, 2003 The vacuolar H+‐ATPases (or V‐ATPases) are a family of ATP‐dependent proton pumps responsible for acidification of intracellular compartments and, in certain cases, proton transport across the plasma membrane of eukaryotic cells. They are multisubunit complexes composed of a peripheral domain (V1) responsible for ATP hydrolysis and an integral domain ...
Kawasaki-Nishi, Shoko +2 more
openaire +2 more sources
Topology of the Yeast Plasma Membrane Proton-translocating ATPase
Journal of Biological Chemistry, 1989 Four proteases have been used to assess the topology of the H+-ATPase from Saccharomyces cerevisiae reconstituted into phosphatidylserine vesicles. Limited proteolysis by trypsin and alpha-chymotrypsin inactivates the enzyme and produces stable, membrane-bound fragments. Sequence analyses of these peptides have located the peptide bonds hydrolyzed. The
C B, Davis, G G, Hammes
openaire +2 more sources
Differential polypeptide synthesis of the proton-translocating ATPase of Escherichia coli [PDF]
Journal of Bacteriology, 1982 We investigated the regulation of the synthesis of the eight polypeptides of the Escherichia coli proton-translocating ATPase. A plasmid carrying the eight genes of the unc operon was used to direct in vivo and in vitro protein synthesis of the eight polypeptides.
W S, Brusilow +2 more
openaire +2 more sources