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  • Title: Insulin binding and degradation studies on erythrocytes at different temperatures.
    Author: Dwenger A, Zick R.
    Journal: Biochim Biophys Acta; 1984 Mar 22; 798(1):132-6. PubMed ID: 6367828.
    Abstract:
    Insulin binding of human erythrocytes has been investigated between 0 and 37 degrees C using porcine 125I-insulin/unlabeled porcine insulin and mono [125I] (Tyr-A14)biosynthetic human insulin/ unlabeled biosynthetic human insulin, respectively. Either system exhibited a regular thermodynamical behavior between 0 and 22 degrees C, giving unitary free-energy changes of about -58/ -59 kJ/mol, unitary entropy changes of about +55/ +70 J/K per mol and a reaction heat of -43.1/ -38.3 kJ/mol. From 22 up to 37 degrees C an irregular thermodynamical behavior could be observed, which can be partially explained by an increased insulin degradation during incubation and an additional time-dependent binding of the degradation products.
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