The effect of Ca 2Ο© -binding protein regucalcin on Ca 2Ο© -ATPase activity in isolated rat liver mitochondria was investigated. The presence of regucalcin (0.1, 0.25, and 0.5 M) in the enzyme reaction mixture led to a significant increase in Ca 2Ο© -ATPase activity. Regucalcin significantly stimulated
Effect of nuclear Ca2+uptake inhibitors on Ca2+-activated DNA fragmentation in rat liver nuclei
β Scribed by Masayoshi Yamaguchi; Kimiko Oishi
- Publisher
- Springer
- Year
- 1995
- Tongue
- English
- Weight
- 515 KB
- Volume
- 148
- Category
- Article
- ISSN
- 0300-8177
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The effect of phorbol 12-myristate 13-acetate (PMA) on Ca2+-ATPase activity in rat h e r nuclei was investigated. Ca2 +-ATPase activity was calculated by subtracting Mg2+ -ATPase activity from (Ca2 +-Mg2 +)-ATPase activity. The nuclear Ca2+-ATPase activity was significantly increased by the presence
The effect of regucalcin, a calcium-binding protein isolated from rat liver cytosol, on Ca2+ transport in rat liver nuclei was investigated. Ca2+ uptake and release were determined with a Ca2+ electrode. Ca2+ uptake increased dependent on adenosine triphosphate (ATP; 0.5-2.0 mM), while the uptake wa