Effect of anti-Ca2+-dependent ATPase sera on the Ca2+-dependent ATPase activity of rabbit skeletal muscle sarcoplasmic reticulum

1989 ◽  
Vol 17 (4) ◽  
pp. 671-673 ◽  
Author(s):  
KAY OHLENDIECK ◽  
NORMA M. RYAN
1983 ◽  
Vol 212 (2) ◽  
pp. 399-405 ◽  
Author(s):  
M D White ◽  
J G Collins ◽  
M A Denborough

The effect of the muscle relaxant dantrolene on isolated sarcoplasmic reticulum was studied in control and malignant-hyperpyrexia-susceptible Landrace pigs. The membranes prepared from both sources showed similar Ca2+-dependent ATPase activities, had comparable phospholipid/protein ratios, and their sodium dodecyl sulphate/polyacrylamide-gel patterns were indistinguishable. Membranes from both sources appeared to bind similar amounts of dantrolene. The drug did not stimulate Ca2+-dependent ATPase activity in preparations from either source. The rates of Ca2+ exchange and Ca2+ efflux appeared to be similar in sarcoplasmic reticulum of control and malignant-hyperpyrexia-susceptible pigs. Dantrolene did not affect either the rates or the amount of Ca2+ lost from the vesicles. These results suggest that dantrolene does not directly affect the movement of Ca2+ across the sarcoplasmic-reticulum membrane.


1981 ◽  
Vol 200 (1) ◽  
pp. 11-15 ◽  
Author(s):  
G N Palexas ◽  
N Savage ◽  
H Isaacs

Denervation of rat skeletal muscle produces after 14 days a decrease in Ca2+ uptake of a heterogeneous population of sarcoplasmic-reticulum vesicles, when measured in the presence of oxalate. The Mg2+-dependent ATPase (Ca2+-independent) activity increased after the same period and the Ca2+ + Mg2+-dependent ATPase activity decreased. Concomitant with these changes, there was an increase in vesicle size and calcium content. The observations are discussed in terms of changes in altered membrane structure, manifested in the shift of the equilibrium of the ATPase from an enzyme involved in calcium transport to a phosphoenzyme giving rise to an increase in the Mg2+-dependent ATPase activity.


Sign in / Sign up

Export Citation Format

Share Document