𝔖 Bobbio Scriptorium
✦   LIBER   ✦

The role of the autoinhibitory domain in differential metal ion activation of calmodulin-stimulated phosphatase

✍ Scribed by Noriko Yokoyama; Jerry H. Wang

Book ID
115930081
Publisher
Elsevier Science
Year
1994
Tongue
English
Weight
552 KB
Volume
337
Category
Article
ISSN
0014-5793

No coin nor oath required. For personal study only.

πŸ“œ SIMILAR VOLUMES

The role of metal ions in the activation
The role of metal ions in the activation of arginase
✍ Megumu Munakata; Syozo Niina; Ikuo Ueda πŸ“‚ Article πŸ“… 1976 πŸ› Elsevier Science βš– 367 KB

The role of metal ions as activators of arginase hydrolyzing arginine were studied. The metal ion is assumed to form a complex with arginine and to promote the enzymatic reaction. The activating ability of the metal ion appears to be governed by the chelating ability and/or the coordination numbers

Divalent cation effects on calcineurin p
Divalent cation effects on calcineurin phosphatase: differential involvement of hydrophobic and metal binding domains in the regulation of the enzyme activity
✍ Ramesh C. Gupta; Ramji L. Khandelwal; Prakash V. Sulakhe πŸ“‚ Article πŸ“… 1990 πŸ› Springer 🌐 English βš– 967 KB

The effects of divalent metals, metal chelators (EDTA, EGTA) and sodium dodecyl sulfate were investigated on the phosphatase activity of isolated bovine brain calcineurin assayed in the absence (called intrinsic) and presence of calmodulin. Intrinsic phosphatase was increased by Mn2+, was unaffected