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  • Journal
    Digital Access
    Provider
    Version
    Oxford
    v. 1-, 1988-
    ScienceDirect
    v. 8-20, 1995-2007.
    Print Access Request
    Location
    Version
    Call Number
    Items
    Stored offsite. Please request print.
    v. 1-7, 1988-94.
    16
  • Article
    Lad PJ, White AA.
    J Cyclic Nucleotide Res. 1979;5(4):315-25.
    Particulate guanylate cyclase from rat lung was stimulated less than 2-fold by agents capable of activating the soluble guanylate cyclase, including sodium nitroprusside, MNNG, azide and hydroxylamine. The action of the first two agents was potentiated by 10 mM 2-mercaptoethanol, and that of the last two by catalase. Pretreatment of the particulate enzyme with the polyene antibiotic, filipin, potentiated the stimulatory effects of the activators, activity with 1 mM nitroprusside in the presence of 2-mercaptoethanol being increased 10.4-fold over basal. The enzyme treated with filipin and nitroprusside showed less specificity for Mn2+, as it was able to use Mg2+ as sole cation more efficiently than the untreated enzyme. Since filipin is known to alter membrane fluidity by interacting with membrane cholesterol, it is proposed that the activity of membrane bound guanylate cylase may be regulated in part by the fluid state of the phospholipid matrix.
    Digital Access Access Options