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  • 1
    ISSN: 0196-9781
    Keywords: Achlorhydria ; Ganglioneuroblastoma ; Ganglioneuroma ; Hypercalcemia ; Hypochlorhydria ; Hypokalemia ; Islet cell hyperplasia ; Multiple endocrine neoplasia ; Neuroblastic tumors ; Neuroblastoma ; Pancreatic endocrine tumor ; Pheochromocytoma ; Tumor localization ; VIP ; VIP radioimmunoassay ; VIP-producing tumor ; WDHA syndrome ; Watery diarrhea
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1432-136X
    Keywords: Key words Melanophore ; Mastoparan ; Compound 48/80 ; GTP-binding protein ; Goldfish ; Carassius auratus
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract  To investigate the functions of GTP-binding protein(s) in the melanosome-aggregating response in fish melanophores, the effects of activators of G-proteins, namely, mastoparan and compound 48/80, were examined in cultured melanophores of the balck-moor goldfish, Carassius auratus. Both mastoparan and compound 48/80 induced an approximately 40% increase in the GTP-hydrolyzing activity in the melanophore membranes compared to the basal level. In intact melanophores, these compounds inhibited the effect of 3-isobutyl-1-methylxanthine, which induced the accumulation of intracellular cAMP. Pretreatment of melanophores with pertussis toxin at 1 μg ⋅ ml-1 for 15 h attenuated the inhibitory effect of mastoparan on the accumulation of cAMP. However, pretreatment with the toxin only slightly attenuated the inhibitory effect of compound 48/80 on the accumulation of cAMP. In addition, compound 48/80 at 1 mg ⋅ ml-1 induced full aggregation of the melanosomes in melanophores, though mastoparan at 5 μmol ⋅ l-1 induced only 10–20% aggregation of melanophores. These results suggest that mastoparan and compound 48/80 can each activate the inhibitory G-protein in goldfish melanophores, which results in inhibition of adenylate cyclase activity. This signal-transduction pathway is involved in the aggregation of melanosomes in these cells.
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 1432-136X
    Keywords: Melanophore ; Mastoparan ; Compound 48/80 ; GTP-binding protein ; Goldfish,Carassius auratus
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract To investigate the functions of GTP-binding protein(s) in the melanosome-aggregating response in fish melanophores, the effects of activators of G-proteins, namely, mastoparan and compound 48/80, were examined in cultured melanophores of the balck-moor goldfish,Carassius auratus. Both mastoparan and compound 48/80 induced an approximately 40% increase in the GTP-hydrolyzing activity in the melanophore membranes compared to the basal level. In intact melanophores, these compounds inhibited the effect of 3-isobutyl-1-methylxanthine, which induced the accumulation of intracellular cAMP. Pretreatment of melanophores with pertussis toxin at 1 μg·ml-1 for 15 h attenuated the inhibitory effect of mastoparan on the accumulation of cAMP. However, pretreatment with the toxin only slightly attenuated the inhibitory effect of compound 48/80 on the accumulation of cAMP. In addition, compound 48/80 at 1 mg·ml-1 induced full aggregation of the melanosomes in melanophores, though mastoparan at 5 μmol·l-1 induced only 10–20% aggregation of melanophores. These results suggest that mastoparan and compound 48/80 can each activate the inhibitory G-protein in goldfish melanophores, which results in inhibition of adenylate cyclase activity. This signal-transduction pathway is involved in the aggregation of melanosomes in these cells.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Springer
    Chromatographia 21 (1986), S. 79-82 
    ISSN: 1612-1112
    Keywords: Thin-layer chromatography ; Column liquid chromatography ; Cellulose conformation ; Hydrophobicity ; DL-amino acids
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Summary For the purpose of biochemical study, the resolution of non-derivatized DL-amino acids was carried out by using native-cellulose thin-layer and column chromatography. Its resolution capability was known to be in proportion to the increase of environmental hydrophobicity. It is suggested that the resolutions of DL-amino acids might be resulted from the cellulose conformation change under hydrophobic conditions. The model structures of cellulose are proposed in order to understand the mechanism of chiral selection of amino acids on its molecular surface.
    Type of Medium: Electronic Resource
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