[Competitive inhibition of Ca-ATPase in the sarcoplasmic reticulum by sodium fluoride].
Effect of NaF and AlCl3 the activity of the sarcoplasmic reticulum Ca-ATP-ase has been investigated. NaF (mM) completely inhibits the Ca-ATP-ase activity in presence of 0.02% tween-20. The inhibition is time- and NaF-concentration-dependent and increases as affected by AlCl3 (microM). The potentiated action of AlCl3 depends on the NaF concentration. AlCl3 without NaF does not change the Ca-ATP-ase activity. NaF inhibits the Ca-ATP-ase competitively with respect to ATP, but NaF plus AlCl3 make the inhibition combined. The affinity of the Ca-ATP-ase to the NaF + AlCl3 complex, but not to NaF decreases by 5 mM with an increase of the Pi concentration. NaF probably interacts with the ATP-binding site and the NaF + AlCl3 complex interacts with the phosphate-binding site of the ATP-ase.
Utegalieva
R S
RS
Ivashchenko
V I
VI
Esyrev
O V
OV
D000535:Aluminum / Q000494:pharmacology; D000077410:Aluminum Chloride; D017607:Aluminum Compounds; D000818:Animals; D000252:Calcium-Transporting ATPases / Q000037:antagonists & inhibitors*; D002712:Chlorides / Q000494:pharmacology; D007700:Kinetics; D011817:Rabbits; D012519:Sarcoplasmic Reticulum / Q000187:drug effects / Q000201:enzymology*; D012969:Sodium Fluoride / Q000494:pharmacology*
D017607:Aluminum Compounds; D002712:Chlorides; D000077410:Aluminum Chloride; D012969:Sodium Fluoride; D000535:Aluminum; D000252:Calcium-Transporting ATPases
Konkurentnoe ingibirovanie Ca-ATP-azy sarkoplazmaticheskogo retikuluma ftoridom natriia.