Ion-stripped bovine brain calmodulin (CaM) binds 4 moles Cd2+ as well as 4 moles Ca2+ per mole protein, with similar affinity; in the presence of 1 mM Mg2+ the molar binding ratio of CaM for Ca2+ decreased to 3, the apparent K0.5 for Ca2+ nearly doubled, but the binding characteristics of CaM for Cd
Metal inhibition of calmodulin activity in monkey brain
โ Scribed by P. J. S. Vig; R. Nath; D. Desaiah
- Book ID
- 102293954
- Publisher
- John Wiley and Sons
- Year
- 1989
- Tongue
- English
- Weight
- 274 KB
- Volume
- 9
- Category
- Article
- ISSN
- 0260-437X
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โฆ Synopsis
Studies were conducted to investigate the effect of vanadium (V5+), cadmium (CdZ+), mercury (Hg2+ ), aluminium (A13+), lead (Pb2') and manganese (Mn") ions on calmodulin (CaMkrelated Ca2'-ATPase activity in rhesus monkey (Macaca mulatta) brain (RMB). The cerebral cortex of RMB was dissected and homogenized in 10% sucrose buffer, and synaptic plasma membranes (SPM) were prepared. Ca2+-ATPase activity was determined by the inorganic phosphate method. Different concentrations of metal ions were incubated with RMB fractions containing endogenous CaM and RMB fractions without CaM. The results show that no metal ion inhibited the basal enzyme but that they showed a profound inhibition of total Ca2' -ATPase containing CaM. The order of potency of metals was Hg>Cd>Pb>Mn>AI>V. Exogenous addition of CaM restored the metal-inhibited enzyme activity to near the normal level. The basal enzyme, when reconstituted with CaM, showed sensitivity to metal ions. These data, presented for the first time in non-human primate brain, indicate that the metal ions inhibit CaM activity in RMB.
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