Unknown

Dataset Information

0

Purification of the synaptosomal plasma membrane (Ca(2+) + Mg(2+))-ATPase from pig brain.


ABSTRACT: The Ca(2+)-ATPase from the synaptosomal plasma membrane has been purified nearly to homogeneity from pig brain by a new procedure involving the calmodulin-affinity-chromatography technique. This is a convenient alternative to the standard methods for the purification of the plasma membrane Ca(2+)-ATPase from different sources that were unsuitable to purify the enzyme from pig brain. The main feature of this procedure is the use of 15% (v/v) glycerol as stabilizing agent, instead of acidic phospholipid. By using this protocol the enzyme was purified 36-fold with respect to the plasma membrane vesicle fraction, showing a specific activity of 2.3 i.u. in the presence of acidic phospholipid. In SDS/PAGE, it appears as a single protein band around Mr140 000 that can be phosphorylated by [gamma-(32)P]ATP in the presence of La(3+) and recognized by specific antibodies against the plasma membrane Ca(2+)-ATPase from pig antral smooth muscle. Calmodulin activates the enzyme 1.5-1.8-fold in the presence of phosphatidylcholine but not in the presence of phosphatidylserine.

SUBMITTER: Salvador JM 

PROVIDER: S-EPMC1217169 | biostudies-other | 1996 Apr

REPOSITORIES: biostudies-other

Similar Datasets

| S-EPMC3493797 | biostudies-literature
| S-EPMC4104672 | biostudies-literature
| S-EPMC1153852 | biostudies-other
| S-EPMC6226504 | biostudies-literature
| S-EPMC6255812 | biostudies-literature
| S-EPMC5613515 | biostudies-literature
| S-EPMC8301758 | biostudies-literature
| S-EPMC1949025 | biostudies-literature
| S-EPMC7930289 | biostudies-literature
| S-EPMC5566957 | biostudies-literature