Proteolytic digestion of Cl--ATPase in rat brain synaptosomes.
- 31 December 1987
- journal article
- research article
- Published by Japan Society for Cell Biology in Cell Structure and Function
- Vol. 13 (2) , 105-111
- https://doi.org/10.1247/csf.13.105
Abstract
Upon tryptic digestion of synaptosomes, ATPase activities decreased in the order of Cl--ATPase ?? Na+, K+-ATPase > anion-insensitive Mg2+-ATPase. Upon synaptosome treatment with hypotonic solution, C1--ATPase or anion-insensitive Mg2+-ATPase was slightly inactivated, while Na+, K+-ATPase underwent a much larger degree of inactivation. ATP-Mg inhibited the ATPase digestion in the hypotonic-solution-treated synaptosomes in a concentration-dependent manner, but not in the untreated synaptosomes. These results suggest that trypsin-digestible site of C1--ATPase are present on both sides of the synaptosomal plasma membrane, and the ATP-Mg binding site of the enzyme is located on the inner surface of the membrane.This publication has 3 references indexed in Scilit:
- Transmembrane orientation of the mannose 6-phosphate receptor in isolated clathrin-coated vesicles.Journal of Biological Chemistry, 1985
- Proteolytic Digestion of Band 3 from Bovine Erythrocyte Membranes in Membrane-Bound and Solubilized States1The Journal of Biochemistry, 1984
- Proteolytic fragmentation of the catalytic subunit of the sodium and potassium adenosine triphosphatase. Alignment of tryptic and chymotryptic fragments and location of sites labeled with ATP and iodoacetateJournal of Biological Chemistry, 1979