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R Whittam

Publications and source records attributed to R Whittam.

45 records · Page 3Linked to original sources
PubMed1967

Physical and chemical reactions of phosphates in red cell membranes in relation to active transport.

1. A study has been made of the chemical reactions associated with the active transport of sodium and potassium in human red cells, with special reference to the action of oligomycin and the labelling of cell membranes by radioactive ATP.2. Oligomycin had the same effects as ouabain on the various aspects of active transport in red cells. It inhibited sodium and potassium transport, the transport ATPase, and the lactate production that is controlled by the sodium pump.3. When cell membranes were incubated with radioactive ATP they became labelled. The labelling, however, was unrelated to the activity of the transport ATPase. Incubation of membranes and intact cells showed that the labelling was a result of physical adsorption of inorganic phosphate to the membranes.4. The results show that if there is a phosphate intermediate in the reaction of the transport ATPase in human red cell membranes, then it is present in amounts too small to be detectable by the methods that have been successfully used with organs such as brain and kidney.

Adenosine Triphosphatases↗
PubMed1966

The mode of inhibition by calcium of cell-membrane adenosine-triphosphatase activity.

1. The mechanism of the inhibition of Na(+)-plus-K(+)-activated adenosine triphosphatase by calcium was investigated with an enzyme preparation from rabbit kidney cortex and with membranes of human erythrocytes. 2. CaATP, rather than ionic Ca(2+), acts as a competitive inhibitor, competing with MgATP in the Na(+)-plus-K(+)-activated adenosine-triphosphatase reaction. 3. There appears to be no competition between calcium and Na(+) for the activation of adenosine triphosphatase. 4. The inhibition of Na(+)-plus-K(+)-activated adenosine triphosphatase of cell membranes by low concentrations of CaATP and the consequent need of intact cells to keep the cytoplasmic concentration of calcium low relative to that of magnesium suggests a raison d'être for the mitochondrial calcium pump.

Adenosine Triphosphatases↗
PubMed1965

The connexion between active cation transport and metabolism in erythrocytes.

1. A study has been made of the dependence on the concentrations of internal Na(+) and external K(+) of lactate and phosphate production in human erythrocytes. 2. Lactate production was stimulated by Na(+) and K(+) but only when they were internal and external respectively. The stimulation was counteracted by ouabain. The production of phosphate was affected in the same way. 3. There is a quantitative correlation between these effects and those previously found for cation movements and the membrane adenosine triphosphatase. 4. It is concluded that the rate of energy production in glycolysis is partly controlled by the magnitude of active transport; the extent of this regulation is shown to vary from 25 to 75% of a basal rate that is independent of active transport. 5. The activity of the membrane adenosine triphosphatase was also compared with rates of Na(+) and K(+) transport. The latter were varied by altering the concentrations of internal Na(+) and external K(+), and by inhibiting with ouabain. 6. A threefold variation of active transport rate was accompanied by a parallel change in the membrane adenosine-triphosphatase activity. The results show a constant stoicheiometry for the number of ions moved/mol. of ATP hydrolysed, independent of the electrochemical gradient against which the ions were moved. 7. Calculations show that the amount of ATP hydrolysed would provide enough energy for the osmotic work. The results are discussed in relation to possible mechanisms for active transport.

Journal Article↗
PubMed1965

Effects of sodium and potassium ions on oxidative phosphorylation in relation to respiratory control by a cell-membrane adenosine triphosphatase.

1. A study has been made of the oxygen consumption of kidney homogenates in relation to the ADP concentration as regulated by the cell-membrane adenosine triphosphatase. Stimulation of this enzymic activity by Na(+) and K(+) caused parallel increases in oxygen consumption and ADP concentration. Similarly, inhibition with ouabain caused a parallel fall. The membrane adenosine triphosphatase concerned in active transport therefore appears to regulate respiration through its control of ADP concentration. 2. The respiration of homogenates and mitochondria was also stimulated by K(+) in a way independent of adenosine-triphosphatase activity. It was shown that K(+) facilitates oxidative phosphorylation and the respiratory response to ADP. A K(+) concentration of 25-50mm was needed for maximum oxidative phosphorylation in the presence of physiological concentration of Na(+). Na(+) counteracted K(+) in the effects on mitochondria. It is concluded that K(+) regulates cellular respiration at two structures, one directly in mitochondria, and the second indirectly through control of ADP production at the cell membrane.

Journal Article↗