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Biomedical subjects

W M Armstrong

Publications and source records attributed to W M Armstrong.

52 records · Page 3Linked to original sources
PubMed1972

Activities of sodium and potassium ions in epithelial cells of small intestine.

Intracellular molar Na(+) activity (a(Na)), measured with cation-selective glass microelectrodes, in epithelial cells of isolated bullfrog small intestine immersed at 26 degrees C in a sodium sulfate Ringer solution containing mannitol was 0.0144 +/- 0.0031 (average value plus or minus standard deviation). The corresponding K(+) activity (a(K)) was 0.0854 +/- 0.0060. Combination of these values with previous estimates of intracellular Na(+) and K(+) concentrations under identical conditions indicated that a substantial fraction of the cellular Na(+) is in an osmotically inactive state. When the cells were exposed to a Ringer solution in which 26 millimoles of mannitol per liter were replaced by 3-O-methyl glucose, highly significant decreases in a(K) and a(Na) were observed. The decrease in a(K) was proportionately larger than the corresponding decrease in a(Na).

Animals↗
PubMed1971

Sodium and potassium activities in normal and "sodium-rich" frog skeletal muscle.

In frog sartorius muscles immersed for 2 hours at 26 degrees C in normal Ringer solution, the intrafiber potassium concentration, C(K)(in millimoles per liter), was 123 +/- 2 (mean value plus or minus standard error), and the potassium activity, a(K) (in millimoles per liter), was 90 +/- 1.0. The corresponding sodium concentration and activity were 20 +/- 1 and 6.5 +/- 0.4, respectively. After overnight immersion in K+-free Ringer solution the values were: CK, 97 +/- 2; aK, 81.5 +/- 1.6; CNa, 47 +/- 2; and aNa, 11.2 +/- 0.6. The changes in aK and aNa during storage were not consistent with an exchange between predominantly "free" fiber K+ and external Na+. These results suggest that the Na+ taken up during overnight immersion largely replaced adsorbed or sequestered K+ in the fibers.

Animals↗
PubMed1967

Discrimination between alkali metal cations by yeast. II. Cation interactions in transport.

K(+) is a competitive inhibitor of the uptake of the other alkali metal cations by yeast. Rb(+) is a competitive inhibitor of K(+) uptake, but Li(+), Na(+), and Cs(+) act like H(+). At relatively low concentrations they behave as apparent noncompetitive inhibitors of K(+) transport, but the inhibition is incomplete. At higher concentrations they inhibit the remaining K(+) transport competitively. Ca(++) and Mg(++) in relatively low concentrations partially inhibit K(+) transport in an apparently noncompetitive manner although their affinity for the transport site is very low. In each case, in concentrations that produce "noncompetitive" inhibition, very little of the inhibiting cation is transported into the cell. Competitive inhibition is accompanied by appreciable uptake of the inhibiting cation. The apparently noncompetitive effect of other cations is reversed by K(+) concentrations much higher than those necessary to essentially "saturate" the transport system. A model is proposed which can account for the inhibition kinetics. This model is based on two cation-binding sites for which cations compete, a carrier or transporting site, and a second nontransporting (modifier) site with a different array of affinities for cations. The association of certain cations with the modifier site leads to a reduction in the turnover of the carrier, the degree of reduction depending on the cation bound to the modifier site and on the cation being transported.

Biological Transport↗