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- W2040353249 abstract "(1) The effects of treatments that mimic calmodulin in increasing the apparent affinity for Ca2+ were tested to see whether, like calmodulin, they also change the activation of the Ca2+-ATPase from human red cell membranes by ATP at the low-affinity site. (2) Short incubations with either trypsin or acidic phospholipids such as phosphatidylserine increased the apparent affinity for ATP at the low-affinity site. (3) Under conditions in which it increased the apparent affinity of the Ca2+-ATPase for Ca2+, EGTA failed to change the activation by ATP. (4) As in calmodulin-bound Ca2+-ATPase, compound 48/80 inhibited the activity of the enzyme in the presence of phosphatidylserine by lowering the apparent affinity for ATP at the low-affinity site, leaving the maximum velocity of the enzyme unaltered. (5) Compound 48/80 also inhibited the Ca2+-ATPase after partial proteolysis, but in this case it lowered the maximum activity, leaving the apparent affinity of the enzyme for ATP at the low-affinity site unaltered. (6) Inhibition of the Ca2+-ATPase by compound 48/80 in the absence of calmodulin suggests that the inhibitor can act directly on the enzyme." @default.
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- W2040353249 date "1989-07-01" @default.
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- W2040353249 title "A study to see whether phosphatidylserine, partial proteolysis and EGTA substitute for calmodulin during activation of the Ca2+-ATPase from red cells membranes by ATP" @default.
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- W2040353249 doi "https://doi.org/10.1016/0167-4838(89)90241-0" @default.
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