Table I.
Effects of Free Mg2+ Ions on Nonactivated PhK
Phk | Effect | References |
---|---|---|
Kinase Activity | ||
6.8 | Time-dependent activation prior to assaya | 3 |
6.8 | Time-dependent activation prior to assay when incubated with phosphorylasea | 4 |
6.8 | Stimulates when in excess over MgATP | 5,6 |
8.2 | Stimulates when in excess over MgATP | 6,7 |
Affinity for Interacting Molecules | ||
6.8 | Alters affinity for Ca2+ plus induces new Ca2+ binding sites | 8 |
7.5 | Increases affinity for glycogen phosphorylase | 9 |
Effects on Specific Subunits | ||
8.2 | Increased ββ1 and αγ conjugates and decreased βγγ in crosslinking by 4-phenyl-1,2,4-triazoline-3,5-dione | 10 |
6.8 | Protects β subunit from trypsinolysis | 11 |
6.8 | Increased binding of mAb γ79 to free γ subunit and to PhK | 12 |
6.8 | Increased binding of mAb γ88 and mAb γ to PhK | 13 |
6.8 | Increased phosphorylation of α subunit at high [Mg2+] by two distinct protein kinases | 14,15 |
Synergistic Effects in Concert with Ca2+ Ions | ||
6.8 | Promotes self-association of PhK | 16–18 |
6.8 | Incubation prior to assays activates kinase | 19 |
6.8 | Promotes formation of β-β dimers in crosslinking by 1,5-difluoro-2,4-dinitrobenzene (DFDNB) | 20 |
6.8 | Incubation prior to assays induces an EGTA- insensitive activity | 21 |
6.8/7.0 | Enhances binding to glycogen | 22–24 |
Without divalent cation chelator.