The effect of Ca 2ฯฉ -binding protein regucalcin on protein kinase activity in the nuclei of normal and regenerating rat livers was investigated. Protein kinase activity in the nuclei isolated from normal rat liver was significantly increased by addition of Ca 2ฯฉ (500 ยตM) and calmodulin (10 ยตg/ml) in
Inhibitory effect of calcium-binding protein regucalcin on protein kinase C activity in rat liver cytosol
โ Scribed by Masayoshi Yamaguchi; Seiichi Mori
- Book ID
- 113382830
- Publisher
- Elsevier Science
- Year
- 1990
- Tongue
- English
- Weight
- 402 KB
- Volume
- 43
- Category
- Article
- ISSN
- 0885-4505
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๐ SIMILAR VOLUMES
The effect of regucalcin, isolated from rat liver cytosol, on neutral proteolytic activity in the hepatic cytosol was investigated. The Ca(2+)-requiring proteinase required 5-10 microM Ca2+ for maximal activity in the presence of a protein substrate (globin). The proteinase activity was markedly ele
The effect of regucalcin, a calcium-binding protein isolated from rat liver cytosol, on Ca2+/calmodulin-dependent cyclic nucleotide (AMP) phosphodiesterase activity in rat liver cytosol was investigated. The addition of Ca2+ (50 microM) and calmodulin 160 U/ml in the enzyme reaction mixture caused a