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  • Title: Purification of a novel isoform of the regulatory subunit of cAMP-dependent protein kinase from the bivalve mollusk Mytilus galloprovincialis.
    Author: Rodríguez JL, Barcia R, Ramos-Martínez JI, Villamarín JA.
    Journal: Arch Biochem Biophys; 1998 Nov 01; 359(1):57-62. PubMed ID: 9799560.
    Abstract:
    Cytosolic extracts from the posterior adductor muscle of the bivalve mollusk Mytilus galloprovincialis contain significant amounts of both cGMP-binding and cGMP-stimulated protein kinase activities. However, photoaffinity labeling with 8-azido-[32P]cGMP revealed only a major cGMP-binding protein with an apparent molecular mass of 54 kDa (p54), lacking protein kinase activity itself. Instead, the purified and cGMP-free p54 protein has the ability to inhibit a mussel protein kinase homologous to the mammalian cAMP-dependent protein kinase (cAPK) catalytic subunit, the inhibition being relieved by cAMP or cGMP, which suggests that it can act as a regulatory subunit of cAPK. However, p54 failed to be recognized by a specific antibody against the regulatory subunit (type RII) previously isolated from mussel. Therefore, p54 must be a novel isoform of cAPK regulatory subunit that seems to have high affinity for both cGMP and cAMP.
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