1. When yeast oxidizes ethanol at different pH values the uptake of K+ corresponds closely to the amount of acetate accumulated at each pH value. 2. The addition of semicarbazide to the suspension buffered at pH4.75 inhibited both the K+ uptake and the acetate accumulation by about 50%. 3. The addition of either acetate or propionate to the suspensions markedly increased the K+ uptake. 4. The addition of acetate to the suspensions lowered the intracellular pH of the yeast from a resting value of pH5.80 to 5.56. 5. The ratio of the initial rate of K+ uptake to O2 consumption was 0.77. This ratio was increased to 1.77 in the presence of 10mmol of propionate/l.
Simultaneous monitoring of ATP synthesis and K+ movements across pea mitochondrial membranes revealed information about the competition of the two processes for mitochondrial energy. In the presence of valinomycin and at low extramitochondrial K+ concentration, ADP could be phosphorylated rapidly. This occurred with a decrease in net potassium ion uptake. At higher external K+ concentrations respiratory energy was unavailable for ATP synthesis and only a portion of added ADP could be phosphorylated within a reasonable time. Magnesium ions were shown to have an inhibitory effect on the K+ uptake, and stimulated a greater rate of ATP synthesis. When valinomycin and ADP were added simultaneously so that phosphorylation of the ADP and enhancement of K+ uptake could compete for mitochondrial energy, K+ uptake was preferred over ATP synthesis.
The phase transformation of MoS2 upon Li, Na, and K ion insertion is systematically explored. The exceptional stability associated with K ion uptake is revealed through complementary experimental and theoretical studies.
Actin is a protein found in all eukaryotic cells. In its polymerized form, the cells use it for motility, cytokinesis and for cytoskeletal support. An example of this latter class is the actin bundle in the acrosomal process from the Limulus sperm. The different functions actin performs seem to arise from its interaction with the actin binding proteins. A 3-dimensional structure of this macromolecular assembly is essential to provide a structural basis for understanding this interaction in relationship to its development and functions.
Clathrin forms the polyhedral cage of coated vesicles, which mediate the transfer of selected membrane components within eukaryotic cells. Clathrin cages and coated vesicles have been extensively studied by electron microscopy of negatively stained preparations and shadowed specimens. From these studies the gross morphology of the outer part of the polyhedral coat has been established and some features of the packing of clathrin trimers into the coat have also been described. However these previous studies have not revealed any internal details about the position of the terminal domain of the clathrin heavy chain, the location of the 100kd-50kd accessory coat proteins or the interactions of the coat with the enclosed membrane.
Five different classes of intermediate-sized filaments (IFs) have been identified in differentiated eukaryotic cells: vimentin in mesenchymal cells, desmin in muscle cells, neurofilaments in nerve cells, glial filaments in glial cells and keratin filaments in epithelial cells. Despite their tissue specificity, all IFs share several common attributes, including immunological crossreactivity, similar morphology (e.g. about 10 nm diameter - hence ‘10-nm filaments’) and the ability to reassemble in vitro from denatured subunits into filaments virtually indistinguishable from those observed in vivo. Further more, despite their proteinchemical heterogeneity (their MWs range from 40 kDa to 200 kDa and their isoelectric points from about 5 to 8), protein and cDNA sequencing of several IF polypeptides (for refs, see 1,2) have provided the framework for a common structural model of all IF subunits.
Mechanism of potassium ion uptake by the Na+/K+-ATPase