Abstract
A Ca2+-dependent, calmodulin-stimulated protein phosphatase (EC 3.1.3.16) is known to be associated with calcineurin, a major calmodulin binding protein in brain. The protein phosphatase activity has now been shown to be retained by a substrate affinity column (thiophosphorylated myosin P-light chain Sepharose) in the presence of Ca2+, and to be eluted specifically with EGTA. Calcineurin behaved identically. This establishes that calcineurin is the Ca2+-dependent protein phosphatase, and that interaction of Ca2+ with the B-subunit is essential for substrate binding.
| Original language | English |
|---|---|
| Pages (from-to) | 191-193 |
| Number of pages | 3 |
| Journal | Biochimica et Biophysica Acta - Proteins and Proteomics |
| Volume | 747 |
| Issue number | 1-2 |
| DOIs | |
| State | Published - 14 Sep 1983 |
| Externally published | Yes |
Keywords
- Affinity chromatography
- Ca-dependent protein phosphatase
- Calcineurin
- Calmodulin binding protein