Cell Structure and Function
Online ISSN : 1347-3700
Print ISSN : 0386-7196
ISSN-L : 0386-7196
Proteolytic Digestion of Cl--ATPase in Rat Brain Synaptosomes
Yukiko Kunugi-UeharaYoshikatsu HashimotoChie OguraChiyoko InagakiTakeshi Nishino
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1988 年 13 巻 2 号 p. 105-111

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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.
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© Japan Society for Cell Biology
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