Pub. Date : 1994 Jan 18
PMID : 8286381
7 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
| 1 | Wheat germ calmodulin was derivatized with rhodamine-x-maleimide. | rhodamine-x-maleimide | CaM5 | Triticum aestivum |
| 2 | The affinity and binding capacity of the channel protein in SR vesicles for the derivatized calmodulin (Rh-CaM) were determined by fluorescence anisotropy in the presence of (1) 1 mM EGTA, (2) 0.1 mM CaCl2, and (3) 0.1 mM CaCl2 plus 1 mM MgCl2. | Egtazic Acid | CaM5 | Triticum aestivum |
| 3 | The affinity and binding capacity of the channel protein in SR vesicles for the derivatized calmodulin (Rh-CaM) were determined by fluorescence anisotropy in the presence of (1) 1 mM EGTA, (2) 0.1 mM CaCl2, and (3) 0.1 mM CaCl2 plus 1 mM MgCl2. | Calcium Chloride | CaM5 | Triticum aestivum |
| 4 | The affinity and binding capacity of the channel protein in SR vesicles for the derivatized calmodulin (Rh-CaM) were determined by fluorescence anisotropy in the presence of (1) 1 mM EGTA, (2) 0.1 mM CaCl2, and (3) 0.1 mM CaCl2 plus 1 mM MgCl2. | Calcium Chloride | CaM5 | Triticum aestivum |
| 5 | The affinity and binding capacity of the channel protein in SR vesicles for the derivatized calmodulin (Rh-CaM) were determined by fluorescence anisotropy in the presence of (1) 1 mM EGTA, (2) 0.1 mM CaCl2, and (3) 0.1 mM CaCl2 plus 1 mM MgCl2. | Magnesium Chloride | CaM5 | Triticum aestivum |
| 6 | In the presence of EGTA, Rh-CaM bound to the channel protein with a Kd of 8.6 +/- 0.8 nM and a Bmax of 229 +/- 7 pmol/mg, suggesting that calmodulin binds to the channel protein at [Ca2+] comparable to that in resting muscle. | Egtazic Acid | CaM5 | Triticum aestivum |
| 7 | In the presence of EGTA, Rh-CaM bound to the channel protein with a Kd of 8.6 +/- 0.8 nM and a Bmax of 229 +/- 7 pmol/mg, suggesting that calmodulin binds to the channel protein at [Ca2+] comparable to that in resting muscle. | rh-cam | CaM5 | Triticum aestivum |