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  • 1
    Digitale Medien
    Digitale Medien
    Amsterdam : Elsevier
    BBA - Protein Structure 625 (1980), S. 318-327 
    ISSN: 0005-2795
    Schlagwort(e): (Anadara broughtonii) ; Allosteric transformation ; Circular dichroism ; Fluorescence spectroscopy ; Hemoglobin ; Ligand binding
    Quelle: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Thema: Biologie
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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  • 2
    ISSN: 1432-0428
    Schlagwort(e): Islet amyloid polypeptide ; amylin ; amidation ; invivo effect ; insulin resistance ; diabetes mellitus
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Medizin
    Notizen: Summary Islet amyloid polypeptide is a 37 amino acid hormone-like peptide which is the major protein component of islet amyloid deposits commonly found in patients with Type 2 (non-insulin-dependent) diabetes mellitus. Recent studies indicate that a physiologically active form of this peptide appears to be carboxyamidated and secreted from the insulin-producing beta cell. In order to clarify the possible in vivo actions of islet amyloid polypeptide, we have studied the effects of synthesized islet amyloid polypeptide-amide on peripheral glucose utilization by performing hyperinsulinaemic euglycaemic glucose clamp studies on dogs. Exogenously administered islet amyloid polypeptide-amide (an infusion from 1.0 to 100 μg·kg−1·h−1, over 2 h) inhibited the insulin-stimulated glucose disposal rate in a dose dependent manner. Twenty-five μg·kg−1·h−1 of islet amyloid polypeptide-amide infused via a peripheral vein significantly lowered the glucose disposal rate by 20% (from 17.4±1.7 to 14.4±1.7 mg·kg−1·min−1, n = 5, p〈0.01). These findings suggest that islet amyloid polypeptide-amide causes peripheral insulin resistance in vivo.
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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