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 |
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Pages (from-to) | 191-193 |
Number of pages | 3 |
Journal | Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular |
Volume | 747 |
Issue number | 1-2 |
DOIs | |
Publication status | Published - 14 Sept 1983 |
Keywords
- Affinity chromatography
- Ca-dependent protein phosphatase
- Calcineurin
- Calmodulin binding protein
ASJC Scopus subject areas
- Biochemistry
- Biophysics
- Molecular Biology
- Structural Biology