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• W2022127097 abstract "The adenylate cyclase activity of Bordetella pertussis culture supernatants is activated 3- to 10-fold by various amphiphiles including many classes of phospholipids and nonionic detergents. Gangliosides are inhibitory. The stimulation affects the Vmax and not the Km. Neither the nature of the polar head group, the length of the fatty acid chains, nor the hydrophile-lipophile balance (in the Triton X series) are major determinants for activation. Short-chain lecithins activate as monomers, whereas long-chain lecithins activate only above the critical micelle concentrations, suggesting high-affinity hydrophobic binding sites. Judged by EGTA inhibition, the amphiphile-mediated activation requires Ca2+ in the absence of calmodulin. In addition, amphiphiles sensitize the adenylate cyclase to Ca2+/calmodulin and are also synergistic with calmodulin for maximal stimulation." @default.
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• W2022127097 date "1982-05-01" @default.
• W2022127097 modified "2023-09-27" @default.
• W2022127097 title "Amphiphile-mediated activation of soluble adenylate cyclase of Bordetella pertussis" @default.
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• W2022127097 doi "https://doi.org/10.1016/0003-9861(82)90111-4" @default.
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