ATPase was detected in the membranes of a motile Streptococcus. Maximal enzymic activity was observed at pH 8 and ATP/Mg 2 Β§ ratio of 2. Mn 2 + and Ca 2 Β§ could replace Mg 2 + to some extent. Besides ATP, GTP and ITP were substrates. The enzyme was inhibited by N,N'-dicyclohexylcarbodiimide but not
β¦ LIBER β¦
A study of sodium release in the course of ATP hydrolysis by membrane ATPase
β Scribed by A. A. Lev; Lidija N. Pisareva
- Publisher
- Springer
- Year
- 1970
- Tongue
- English
- Weight
- 692 KB
- Volume
- 2
- Category
- Article
- ISSN
- 0022-2631
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## Abstract A role of __ATP13A2__ in earlyβonset Parkinsonism (EOP) has been proposed. Conversely, the contribution of this ATPase to lateβonset Parkinson's disease (PD) remains unexplored. We therefore conducted a caseβcontrol association study in this ageβofβonset group with PD. The initial sampl