Key result
Upon addition of EGTA in the absence of ATP, about 50% of the Ca bound to the transport sites of sarcoplasmic reticulum is rapidly dissociated, whereas the rest dissociates slowly.
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The study demonstrates nonequivalent subunits in the calcium pump of the sarcoplasmic reticulum based on differential calcium dissociation rates.
Rapid mixing chemical quench studies of the Ca2+-ATPase reaction of fragmented sarcoplasmic reticulum were carried out at low temperatures (2-4 "C) in order to facilitate kinetic analysis.Upon addition of ethylene glycol bis( #Laminoethyl ether)-N,N,N',N'-tetraacetic acid (EGTA) in the absence of ATP, about 50% of the Ca bound to the transport sites is rapidly dissociated, whereas the rest dissociates slowly (k 2.5 s-'), as ' The abbreviations used are: SR, sarcoplasmic reticulum; EGTA, ethylene glycol bis(P-aminoethyl ether)-N,N,N',N'-tetraacetic acid; CY&, dodecyloctaoxyethylene glycol monoether; EP, phosphorylated intermediate of enzyme; Mops, morpholinopropane sulfonic acid; RBS, reaction base solution.
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Ikemoto et al. (1981) studied this question. EGTA was evaluated on Ca dissociation. Upon addition of EGTA in the absence of ATP, about 50% of the Ca bound to the transport sites of sarcoplasmic reticulum is rapidly dissociated, whereas the rest dissociates slowly.
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