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World J Biol Chem. Mar 26, 2011; 2(3): 39-47
Published online Mar 26, 2011. doi: 10.4331/wjbc.v2.i3.39
Published online Mar 26, 2011. doi: 10.4331/wjbc.v2.i3.39
Figure 2 Caloxin 2A1 inhibition of plasma membrane Ca2+ pump ATPase in the erythrocyte ghosts is non-competitive with respect to Ca2+, ATP and calmodulin[22].
The percent inhibition with caloxin 2a1 (1.8 mmol/L) did not differ significantly between low or high concentration of Ca2+. Similarly, concentrations of ATP and calmodulin did not influence the percent inhibition with caloxin 2a1. The low and high concentrations compared for each ligand are shown. Concentrations of all the other ligands were saturating in each experiment. Details of the experiments are available in[22].
- Citation: Pande J, Szewczyk MM, Grover AK. Allosteric inhibitors of plasma membrane Ca2+ pumps: Invention and applications of caloxins. World J Biol Chem 2011; 2(3): 39-47
- URL: https://www.wjgnet.com/1949-8454/full/v2/i3/39.htm
- DOI: https://dx.doi.org/10.4331/wjbc.v2.i3.39