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- W2091375262 abstract "A neutral pH-optimum sphingomyelinase (N-SMase), solubilized from rat brain membranes, was characterized with respect to metal and membrane lipid effects. Chromatofocusing chromatography, which separates proteins according to pI, showed two N-SMase activities. One eluted at pH 4.7 and the other required 0.4 M NaCl before elution. Kinetically, the two preparations appeared similar. The N-SMase eluting at pH 4.7 was most extensively studied here. Of the phospholipids studied, only phosphatidylserine showed any influence on N-SMase and that was to increase its activity by as much as 50%. Neither serine nor phosphatidic acid had any effect. Of the cations tested, none was able to replace Mg2+ as a required activator. However, it was found that several metals were inhibitory, with Cu2+ being most effective (IC50 = 5 microM). Gangliosides, particularly the monosialoganglioside, GM3 (IC50 approximately 50 microM), inhibited N-SMase. Other glycolipids showed little effect on activity, even the immediate precursor to GM3 - lactosylceramide. The ganglioside sugar, N-acetylneuraminic acid, also had no effect on N-SMase activity. None of these inhibitors affected the acidic pH-optimum sphingomyelinase. Other sphingolipid compounds such as ceramide - the enzymatic product - and sphingosylphosphorylcholine (lysosphingomyelin) showed no capacity to inhibit N-Smase, implying that the enzyme may have a selective substrate-binding site." @default.
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- W2091375262 date "1993-01-01" @default.
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- W2091375262 title "Characterization of the neutral pH-optimum sphingomyelinase from rat brain: Inhibition by copper II and ganglioside GM3" @default.
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- W2091375262 doi "https://doi.org/10.1016/0005-2760(93)90142-v" @default.
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