Electron cytochemistry of oxalate-stimulated calcium uptake in microsomes from the smooth muscle of the pig stomach

1980 ◽  
Vol 65 (2) ◽  
pp. 121-129 ◽  
Author(s):  
L. Raeymaekers ◽  
B. Agostini ◽  
W. Hasselbach
1980 ◽  
Vol 595 (2) ◽  
pp. 309-312 ◽  
Author(s):  
Bella T. Altura ◽  
Prasad D.M.V. Turlapaty ◽  
Burton M. Altura

1982 ◽  
Vol 242 (3) ◽  
pp. C242-C249 ◽  
Author(s):  
G. D. Ford ◽  
M. L. Hess

A vesicular fraction isolated from bovine aorta and enriched in fragmented sarcoplasmic reticulum (FSR) exhibited active calcium transport and ATPase activity. By use of a hypotonic NaHCO3 extraction solution, an active preparation was isolated that retained activity for up to 4 days. A small but significant (P less than 0.05) Ca2+-stimulated, Mg2+-dependent ATPase associated with calcium transport was demonstrated with a specific activity of 0.33 mumol inorganic phosphate (Pi).mg-1.min-1. The basal Mg2+ ATPase demonstrated Michaelis-Menten kinetics [Km(Mg2+-ATP) = 0.44 +/- 0.01 X 10(-3) M; Vmax = 2.22 +/- 0.01 mumolPi.mg-1.min-1]. The Ca2+-stimulated, Mg2+-ATPase demonstrated apparent substrate inhibition (Ks approximately 10 mM) with no evidence for end-product (ADP) or excess added Ca2+ contributing to this inhibition. Oxalate-supported active calcium uptake velocities also exhibited quantitatively similar substrate inhibition. These results suggest that FSR from vascular smooth muscle contains either two enzymes or one enzyme with two isomeric forms, one of which is associated with the calcium uptake activity of this structure and the other of unknown function.


1976 ◽  
Vol 40 (10) ◽  
pp. 1175-1181 ◽  
Author(s):  
KANAE YAMASHITA ◽  
KYUZO AOKI ◽  
KIYOHARU TAKIKAWA ◽  
KEN HOTTA

Cell Calcium ◽  
1984 ◽  
Vol 5 (3) ◽  
pp. 205-210 ◽  
Author(s):  
L. Raeymaekers ◽  
R. Casteels
Keyword(s):  

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