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Adenylate cyclase of Mytilus galloprovincialis posterior adductor muscle: basal properties and sensitivity to serotonin

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Abstract

The presence and characteristics of a membrane-bound adenylate cyclase from Mytilus galloprovincialis Lmk posterior adductor muscle have been investigated. The enzyme has a Michaelis constant (K m) of 0.38 mM at 20°C and requires divalent cations (Mg2+/Mn2+) for its activity. Optimal GTP concentrations are between 10-5 and 10-4 M. The non-hydrolizable GTP-analogues GMPpNHp and GTPγS increase the activity of the enzyme four- to ten-fold. Sodium fluoride stimulates the enzymatic activity seven- to eight-fold. Forskolin increases the enzymatic activity two- to three-fold. Serotonin stimulates the adenylate cyclase activity in a dose-dependent manner. These experiments were performed with mussels collected from the estuary of Muros, Spain, in 1990.

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Authors and Affiliations

  1. Department of Physiology, Faculty of Pharmacy, University of Santiago de Compostela, E-15706, Santiago de Compostela, Spain

    M. Treviño, M. J. Mancebo, E. J. Ferran & J. Espinosa

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  1. M. Treviño
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  2. M. J. Mancebo
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  3. E. J. Ferran
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  4. J. Espinosa
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Communicated by O. Kinne, Oldendorf/Luhe

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Treviño, M., Mancebo, M.J., Ferran, E.J. et al. Adenylate cyclase of Mytilus galloprovincialis posterior adductor muscle: basal properties and sensitivity to serotonin. Marine Biology 115, 407–412 (1993). https://doi.org/10.1007/BF00349839

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  • DOI: https://doi.org/10.1007/BF00349839

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