3.4.22.53 Al3+ millimolar concentrations of Al3+ activate at at submillimolar concentrations of Ca2+ 644005 3.4.22.53 Ba2+ 1 mM, decreases the Ca2+-requirement for maximal activity from 0.4 mM to 0.3 mM. Synergistic activating effect with Ca2+ 644027 3.4.22.53 Ba2+ 5 mM 85.4% of the activation with 5 mM Ca2+ 644026 3.4.22.53 Ba2+ 5 mM, activates 644031 3.4.22.53 Ba2+ activates 644052 3.4.22.53 Ba2+ slight activation 643987 3.4.22.53 Ca2+ - 643982 3.4.22.53 Ca2+ 0.4 mM Ca2+ is required for 50% caseinolysis of recombinant enzyme 644029 3.4.22.53 Ca2+ 3 mM used in assay conditions 732375 3.4.22.53 Ca2+ 5 mM required for optimal activity 644046 3.4.22.53 Ca2+ absolute requirement 644025 3.4.22.53 Ca2+ activated by Ca2+ 732365 3.4.22.53 Ca2+ activates 644026, 717806 3.4.22.53 Ca2+ activates. The results support the hypothesis that Ca2+ induces movement of domains I and II closer together to form the functional active site of calpain 644017 3.4.22.53 Ca2+ best activator at 2.5 mM, maximal caseinolytic activity at 2.2 mM, half-maximal caseinolytic activity at 0.312 mM 644052 3.4.22.53 Ca2+ Ca2+ induces calpain translocation to the membrane during ischemia 709566 3.4.22.53 Ca2+ Ca2+-binding must induce conformational changes that reorient the protease domains to form a functional active site 644020 3.4.22.53 Ca2+ Ca2+-induced calpain translocation to the membrane during ischemia is independent of its activation 709566 3.4.22.53 Ca2+ calcium-dependent cysteine protease 708416 3.4.22.53 Ca2+ calpain 2 is activated with addition of CaCl+ to 1 mM 709126 3.4.22.53 Ca2+ dependent on 665705, 707281, 707372, 707385, 709031, 709540, 709927 3.4.22.53 Ca2+ half maximal activity for retina and brain enzyme is 0.262 mM and 0.311 mM, maximal activity near 1 mM, no activity in presence of 0.03 mM 644030 3.4.22.53 Ca2+ half-maximal activation at 0.15 mM, maximal activation at 1 mM 643983 3.4.22.53 Ca2+ half-maximal activation at 0.2 mM, full activity at 1 mM 643987 3.4.22.53 Ca2+ half-maximal activation at 0.2 mM, maximal activation at 1 mM 643981 3.4.22.53 Ca2+ half-maximal activation at 0.5 mM 643977 3.4.22.53 Ca2+ half-maximal activation at 0.8 mM, maximal activation at 1.5 mM 643980 3.4.22.53 Ca2+ half-maximal activity at 0.18 mM 643986 3.4.22.53 Ca2+ half-maximal activity at 0.23 mM, maximal activity at 1-2.5 mM 644031 3.4.22.53 Ca2+ half-maximal activity at 0.4 mM, maximal activity at 1.5 mM 644027 3.4.22.53 Ca2+ half-maximal activity at 2.4 mM, maximal activity at 5 mM 644031 3.4.22.53 Ca2+ half-maximal activity is 0.242 mM for wilde-type enzyme, 0.129 mM for the E504S mutant, 0.226 mM for the K226S mutant, 0.261 mM for the K230S mutant, 0.183 mM for the K234 mutant, 0.256 mM for the K230E mutant and 0.159 mM for the K234E mutant 644019 3.4.22.53 Ca2+ half-maximal activity of wild-type enzyme at 0.242 mM 644019 3.4.22.53 Ca2+ Ka-value: 0.7 mM 643988 3.4.22.53 Ca2+ Kd-value: 0.325 mM. 25% of the difference in Kd values between mu-calpain and m-calpain can be ascribed to the N-terminal peptide of the large subunit, whereas the C-terminal EF-hand-containing domain IV accounts for 65% of the difference 643968 3.4.22.53 Ca2+ maximum calcium requirement of 0.6 mM 717623 3.4.22.53 Ca2+ optimum activity at 5 mM Ca2+ 708960 3.4.22.53 Ca2+ required 688496, 752437 3.4.22.53 Ca2+ required for activity 709013, 717628, 718169, 718262 3.4.22.53 Ca2+ requires approximately 0.3 mM Ca2+ for half-maximal activity in vivo 706941 3.4.22.53 Ca2+ requires millimolar calcium concentrations for activation 709641 3.4.22.53 Ca2+ requires millimolar order calcium ions for activation 644032 3.4.22.53 Ca2+ the Ca2+ dependency of mitochondrial m-calpain is similar to that of cytosolic m-calpain, 1 mM Ca2+ activates. 707559 3.4.22.53 Ca2+ treatment of the endoplasmic reticulum with Ca2+ (5 mM) dissociates m-calpain-calpastatin association leading to the activation of m-calpain 708954 3.4.22.53 Ca2+ wild-type enzyme has a Kd-value of 0.325 mM 644047 3.4.22.53 Co2+ 5 mM, activates 644031 3.4.22.53 Cu2+ activates 644052 3.4.22.53 K+ 5 mM, activates in presence of 5 mM Ca2+ 644031 3.4.22.53 Mg2+ 1 mM decreases the Ca2+-requirement for maximal activity from 0.4 mM to 0.3 mM. Synergistic activating effect with Ca2+ 644027 3.4.22.53 Mg2+ 5 mM, activates in presence of 5 mM Ca2+ 644031 3.4.22.53 Mg2+ slight activation 643987 3.4.22.53 Mn2+ 1 mM, decreases the half-maximal Ca2+-requirement from 0.4 mM to 0.1 mM, decreases the Ca2+-requirement for maximal activity from 1.5 mM to 1 mM 644027 3.4.22.53 Mn2+ 5 mM 73.6% of the activation with 5 mM Ca2+. Synergistic activating effect with Ca2+ 644026 3.4.22.53 Mn2+ 5 mM, activates 644031 3.4.22.53 Mn2+ activates 644052 3.4.22.53 Na+ 5 mM, activates in presence of 5 mM Ca2+ 644031 3.4.22.53 Sr2+ 1 mM, decreases the half-maximal Ca2+-requirement from 0.4 mM to 0.1 mM, decreases the Ca2+-requirement for maximal activity from 1.5 mM to 1 mM. Synergistic activating effect with Ca2+ 644027 3.4.22.53 Sr2+ 2.5 mM, 66% of the activation obtained with Ca2+, maximal caseinolytic activity at 5.9 mM, half-maximal caseinolytic activity at 1.886 mM. Autolysis in presence of 5 mM Ca2+. The 80000 Da subunit is rapidly autolyzed in two smaller bands of 73000 Da and 69000 Da. The small subunit of 24000 da is degraded into three bands of 22000 Da, 19300 Da and 17800 Da. It is not clear whether autolysis is necessary for calpain to become proteolytically active 644052 3.4.22.53 Sr2+ 5 mM 91% of the activation with 5 mM Ca2+ 644026 3.4.22.53 Sr2+ 5 mM, activates 644031 3.4.22.53 Sr2+ activates 643987 3.4.22.53 Sr2+ activates, Ka: 5.1 mM 643988