Solubilization and reconstitution of the calcium release channel of skeletal sarcoplasmic reticulum.
Fragmented heavy sarcoplasmic reticulum was solubilized by cholate, and proteins were subsequently fractionated by using diethylaminoethyl-cellulose (DEAE-cellulose) column chromatography. A fraction was collected in which proteins with molecular weights between 31,000 and 45,000 u were major components. This fraction, when incorporated into Ca2+ -loaded liposomes, facilitated the Ca2+ efflux. The rate of efflux was regulated by the external Ca2+ concentration, reaching a maximum at 3 microM Ca2+. The Ca2+ efflux was suppressed by Mg2+.
Ohnishi
S T
ST
Horiuchi
K Y
KY
Horiuchi
K
K
D000818:Animals; D002118:Calcium / Q000378:metabolism*; D066298:In Vitro Techniques; D007473:Ion Channels / Q000032:analysis / Q000378:metabolism*; D008081:Liposomes; D008970:Molecular Weight; D009132:Muscles / Q000378:metabolism; D011506:Proteins / Q000302:isolation & purification; D011817:Rabbits; D012519:Sarcoplasmic Reticulum / Q000378:metabolism*
D007473:Ion Channels; D008081:Liposomes; D011506:Proteins; D002118:Calcium