Increased sodium plus potassium adenosine triphosphatase activity in erythrocyte membranes in Huntington's disease

1978 ◽  
Vol 4 (1) ◽  
pp. 60-62 ◽  
Author(s):  
D. A. Butterfield ◽  
J. Q. Oeswein ◽  
M. E. Prunty ◽  
K. C. Hisle ◽  
W. R. Markesbery
1981 ◽  
Vol 44 (7) ◽  
pp. 570-573 ◽  
Author(s):  
T. M. Dubbelman ◽  
A. W D. Bruijne ◽  
J. V. Steveninck ◽  
G. W Bruyn

Author(s):  
D. Allan Butterfield ◽  
James Q. Oeswein ◽  
William R. Markesbery

1973 ◽  
Vol 45 (6) ◽  
pp. 775-784 ◽  
Author(s):  
C. H. Cole

1. Ouabain-sensitive ATPase (adenosine triphosphatase) activity was measured in the erythrocyte membranes of twenty patients with chronic renal disease. Decreased activity was found in nineteen of the twenty patients. The average decrease was 38%. 2. In three patients erythrocyte sodium concentration exceeded 9·5 mmol/l of RBC and these patients had the most marked decreases in ouabain-sensitive ATPase activity. 3. By contrast, in only two of 100 patients admitted to a general medical ward was erythrocyte sodium concentration greater than 9.5 mmol/l of RBC. 4. Ouabain-insensitive and calcium-activated components of erythrocyte membrane ATPase were unaffected by chronic renal disease.


1968 ◽  
Vol 109 (3) ◽  
pp. 369-374 ◽  
Author(s):  
R. N. Priestland ◽  
R. Whittam

1. A study has been made of the interaction between Na+ and K+ on the adenosine triphosphatase activity of erythrocyte ‘ghosts’, and on the K+ influx and Na+ efflux of intact erythrocytes. The adenosine triphosphatase activity and the ion movements were greater at a low external K+ concentration in the absence of Na+ than they were in the presence of 150mm-Na+. The inhibition by external Na+ of K+ influx had an inhibitory constant of 5–10mm. 2. Activation by K+ of kidney microsomal adenosine triphosphatase was retarded by Na+, and activation by Na+ was retarded by K+. Fragmented erythrocyte membranes behaved similarly. 3. These observations suggest that there is competition between Na+ and K+ at the K+-sensitive site of the membrane.


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