Solubilization of a high affinity CA-ATPase from dog antrum smooth muscle.
A Mg-independent high affinity Ca-ATPase has recently been reported to be present in the plasma membranes of smooth muscle. This enzyme has now been solubilized using deoxycholate. The membrane-bound and the solubilized enzymes resemble each other in Km for Ca2+, and inhibition by fluphenazine. The solubilized enzyme is, however, more sensitive to inhibition by Mg2+ than the membrane bound enzyme. Radiation inactivation analysis shows that whereas the membrane-bound enzyme had a target size of 98,000 +/- 4,000 Daltons, the solubilized enzyme was only 70,000, +/- 7,000 Daltons.
Grover
A K
AK
Oakes
P J
PJ
Samson
S
S
Berenski
C J
CJ
Jung
C Y
CY
D000201:Activation Analysis; D000818:Animals; D002118:Calcium / Q000494:pharmacology; D000252:Calcium-Transporting ATPases / Q000032:analysis*; D002462:Cell Membrane / Q000201:enzymology; D003840:Deoxycholic Acid; D004285:Dogs; D008274:Magnesium / Q000378:metabolism / Q000494:pharmacology; D008970:Molecular Weight; D009130:Muscle, Smooth / Q000201:enzymology*; D011706:Pyloric Antrum / Q000201:enzymology; D012995:Solubility
D003840:Deoxycholic Acid; D000252:Calcium-Transporting ATPases; D008274:Magnesium; D002118:Calcium