Hydrodynamic molecular weight of solubilized cholinergic synaptic vesicle glycoprotein ATPase.
The Torpedo californica electric organ synaptic vesicle glycoprotein ATPase was solubilized with octaethyleneglycoldodecyl ether and stabilized with phosphatidylserine. The complex was analyzed by size exclusion chromatography and band sedimentation velocity ultracentrifugation in water/glycerol and deuterium oxide/glycerol density gradients. The complex was found to have a Stokes' radius of 79 +/- 0.7 A, a sedimentation velocity coefficient at 20 degrees C in water of 6.8 +/- 0.2S, a partial specific volume of 0.81 +/- 0.01 cm3/g, and a frictional coefficient of 1.6. The molecular weight of the solubilized complex was calculated to be 320,000 +/- 7,000 and that of the protein 210,000 +/- 9,000. The relationship of this latter value to the major transport ATPase types is discussed.
Yamagata
S K
SK
Department of Chemistry, University of California, Santa Barbara 93106.
Parsons
S M
SM
D000251:Adenosine Triphosphatases / Q000378:metabolism*; D000818:Animals; D002799:Cholinergic Fibers / Q000166:cytology*; D008433:Mathematics; D008970:Molecular Weight; D012995:Solubility; D013572:Synaptic Vesicles / Q000201:enzymology*; D014101:Torpedo; D014461:Ultracentrifugation
D000251:Adenosine Triphosphatases