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  • 1
    ISSN: 1420-9071
    Keywords: Melatonin ; hypophysectomy ; ACTH-derived peptides ; benzodiazepine receptor ; brain
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract In this study, we examined the effect of intracerebroventricular (i.c.v) injection of melatonin and/or ACTH1–10 and ACTH4–10 on [3H]flunitrazepam binding sites in the cerebral cortex of hypophysectomized rats. Hypophysectomy increased the Bmax (maximum number of binding sites) of benzodiazepine (BNZ) receptors for at least 7 days after surgery, without changing KD (dissociation constant). The i.c.v. injection of melatonin to hypophysectomized rats significantly increased Bmax, whereas the same doses of melatonin were ineffective in sham-operated animals. In both cases, KD values were unchanged. The i.c.v injection of ACTH1–10 to hypophysectomized animals significantly increased Bmax, an effect that was enhanced by simultaneous i.c.v. injection of ACTH1–10+melatonin, reaching higher values of Bmax than the i.c.v. injection of these hormones individually. No significant changes in KD values were found after ACTH1–10 and/or melatonin administration. However, the i.c.v. injection of ACTH4–10 to hypophysectomized rats did not change Bmax, although it significantly increased KD values, indicating a decrease in the BNZ binding affinity. Melatonin injection counteracted this effect of ACTH4–10, returning KD to the control value. Moreover, although the lower dose of i.c.v. melatonin used, 10 ng, was unable to modify Bmax of BNZ binding in the ACTH4–10-injected group, the higher dose, 20 ng, significantly increased Bmax. The results suggest that these ACTH-derived peptides can modulate the effect of melatonin on brain benzodiazepine receptors.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1573-8272
    Keywords: peroxidase ; African oil palm ; leaves ; purification ; stability
    Source: Springer Online Journal Archives 1860-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract In the previous work, after screening tropical plants (43 species) for peroxidase activity, high activity has been detected in leaves of some palms and especially African oil palm Elaeis guineensis. This palm is widely cultivated in Colombia and presents a promising source for the industrial production of peroxidase. The initial enzyme isolation included homogenization and extraction of pigments using aqueous two phase polymer system. Initially, traditional system, formed by polyethyleneglycol/K2HPO4, was used. The replacement of K2HPO4 with (NH4)2SO4 allowed direct application of the salt phase with accumulated peroxidase on a Phenyl-Sepharose column. The final purification was carried out by liquid chromatography on Sephacryl S200 and DEAE-Toyopearl columns. The specific activity of the purified peroxidase measured toward guaiacol was 4300 units per mg of protein. The molecular weight and isoelectric point for palm peroxidase were 57.000 and 3.8, respectively. Palm peroxidase possesses uniquely high thermostability and is more stable in organic solvents than horseradish peroxidase is.
    Type of Medium: Electronic Resource
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