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Dependence of rat serum lactonase upon calcium

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References (5)

  • R.H. Roth et al.

    Biochem. Pharmac.

    (1965)
  • P. Henry

    Z. phys. Chem.

    (1892)
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Cited by (29)

  • Impact of strain, sex, and estrous cycle on gamma butyrolactone-evoked absence seizures in rats

    2018, Epilepsy Research
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    GBL induces AS across species, including mouse, rat, non-human primate, and humans (although see (Venzi et al., 2015) for caveats regarding this model in mice). GBL is biologically inactive (Snead, 1991) but is rapidly converted into gamma-hydroxybutyric acid (GHB) by active lactonases present in serum and liver (Roth et al., 1967). Systemic administration of GBL reliably meets all criteria of an absence seizure model in rats (Snead, 1992a, 1988, 1984) and produces electrographic and behavioral events similar to human absence seizures (Cortez et al., 2016; Crunelli and Leresche, 2002).

  • Acute and chronic pharmacological models of generalized absence seizures

    2016, Journal of Neuroscience Methods
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    GBL has been shown to be biologically inactive (Roth et al., 1966; Snead, 1991). An active lactonase that rapidly converts GBL to GHB is present in serum and liver, but not brain or cerebrospinal fluid (Roth and Giarman, 1966; Roth et al., 1967). GBL is used because of the consistency and rapidity of onset of its effect (Bearden et al., 1980) and has been shown to produce exactly the same EEG and behavioral effect as that of GHB (Snead and Bearden, 1980; Snead, 1991).

  • Gamma hydroxybutyrate (GHB), gamma butyrolactone (GBL) and 1,4-butanediol (1,4-BD; BDO): A literature review with a focus on UK fatalities related to non-medical use

    2015, Neuroscience and Biobehavioral Reviews
    Citation Excerpt :

    The pathway of GHB production after death remains unclear and it has also been suggested that GHB can be a product of post-mortem decomposition (Fieler et al., 1998; Sakurada et al., 2002). GBL is metabolised quickly to GHB by peripheral calcium dependent serum lactonases or by nonenzymatic hydrolysis (Arena and Fung, 1980; Roth and Giarman, 1965; Roth et al., 1967); the half-life of this conversion being estimated as <1 min (Roth and Giarman, 1966). Time to peak serum concentration of GBL is 36–57 min, with an elimination half-life of 30–52 min (Meyer et al., 2014a,b).

  • Divergence and convergence in enzyme evolution: Parallel evolution of paraoxonases from quorum-quenching lactonases

    2012, Journal of Biological Chemistry
    Citation Excerpt :

    As is the case with PLLs, the identification of serum paraoxonases (PONs) and the family's name relate to their paraoxon-hydrolyzing activity. Although the earliest identification might have been of a lactonase (48), it was only much later realized that PONs are in fact lactonases (49, 50) that also exhibit some quorum-quenching activity (51). The paraoxonase activity exhibited by PONs turned out to be a promiscuous coincidental activity (50, 52).

  • Behavioral analyses of GHB: Receptor mechanisms

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