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- W2029967575 abstract "Abstract A comparison was made between the activation of membrane-bound adenylate cyclase from rat fat cell membranes and the enzyme solubilized with digitonin. The isoprenaline stimulation of the particulate enzyme was enhanced by GTP, both in the presence of Mg2+ and Mn2+, but no effect of the metal ion nor of GTP was found on the Ka of isoprenaline. The Ka of sodium fluoride for enzyme stimulation was shifted to 3-fold higher concentrations when Mg2+ was replaced by Mn2+, whereas V decreased. GTP did not influence the Ka of sodium fluoride but reduced V, irrespective of the metal ion. After digitonin solubilization the enzyme was no longer responsive to isoprenaline or GTP; however, V of the sodium fluoride activation was higher in the presence of Mn2+ than in the presence of Mg2+, and the Ka was found at 15-fold higher concentrations. Both the solubilized and the particulate adenylate cyclase were inhibited by adenosine; this inhibition was also seen with the fluoride stimulated enzyme. We conclude that solubilization with digitonin did not result in an enzyme preparation which preferentially turns over MnATP2+, although the fat cell adenylate cyclase possesses a metal ion regulatory site with a higher affinity for Mn2+ than for Mg2+. The data suggest that the guanyl nucleotide regulatory site and the sodium fluoride-sensitive site are located on different subunits while there is an interaction between the metal ion regulatory site and the fluoride-sensitive site." @default.
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- W2029967575 date "1981-06-01" @default.
- W2029967575 modified "2023-09-27" @default.
- W2029967575 title "The influence of the divalent cations Mn2+ and Mg2+ on the activation of particulate and digitonin-solubilized adenylate cyclase from rat fat cell membranes" @default.
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- W2029967575 doi "https://doi.org/10.1016/0003-9861(81)90278-2" @default.
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