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  • Insulin receptor  (1)
  • stimulation of insulin release by cyclic-AMP and tolbutamide  (1)
  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Diabetologia 9 (1973), S. 251-254 
    ISSN: 1432-0428
    Keywords: Human insulinoma ; culture of dissociated tumorβ-cells ; insulin release in culture ; stimulation of insulin release by cyclic-AMP and tolbutamide
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Tumor cells from two human insulinomas were maintained in culture for more than 6 months. The cultured cells synthesized and secreted proinsulin and insulin; and responded to cyclic AMP (1 mM) and tolbutamide (1 mM) stimulation with increased insulin release. In culture, these cells did not respond to stimulation by high concentrations of glucose (300 mg%) or by glucagon (10 μg/ml).
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Diabetologia 28 (1985), S. 786-792 
    ISSN: 1432-0428
    Keywords: Insulin receptor ; α-subunit ; insulin binding
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Photoaffinity labelling of hepatic insulin receptors revealed specifically-labelled bands of 130, 90 and 40kDa. Endogenous protease activity in hepatic plasma membranes, as well as contaminating proteases present in preparations of clostridial collagenase, degraded some of the 130-kDa insulinbinding subunit to a 115-kDa form. However, a large proportion of the 130-kDa subunits were resistant to degradation, suggesting the presence of two classes of insulin receptor in hepatic plasma membranes. In one class the 130-kDa subunit was sensitive to proteolysis, while in the other it was not. In contrast, the 130-kDa receptor subunits of adipose tissue were all resistant to such degradation. Scatchard analysis of control and collagenase-treated plasma membranes demonstrated that conversion of the 130-kDa subunit to a 115-kDa form did not affect the insulin-binding characteristics of the receptor. It was also apparent that insulin binds to a single class of highaffinity sites in hepatic plasma membranes.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
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