Library

feed icon rss

Your email was sent successfully. Check your inbox.

An error occurred while sending the email. Please try again.

Proceed reservation?

Export
  • 1
    ISSN: 1432-0428
    Keywords: Insulin ; glucagon ; receptors ; adenylate cyclase ; radioreceptorassay ; bioassay ; radioimmunoassay ; liver membranes ; fat cells ; genetically obese rat (fatty)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Insulin, proinsulin and glucagon extracted from lean rat pancreases were studied in radioimmunoassay, radioreceptorassay and bioassay systems. Extracted insulin behaved identically to a rat insulin used as a reference standard in radioimmunoassay. On the basis of its immunoreactivity, extracted insulin was slightly less potent (about 70%) than the rat standard insulin in competing with the binding of125I-insulin to rat liver membranes (radioreceptorassay) and in stimulating glucose oxidation by rat fat cells (bioassay). Extracted glucagon and a pork glucagon used as a reference standard were indistinguishable in two radioimmunoassay systems for glucagon, in competing with the binding of125I-glucagon to rat liver membranes (radioreceptorassay) and in stimulating adenylate cyclase in rat liver membranes (bioassay). Genetically obese rats (Zucker, “fatty”) were compared to their lean littermates with respect to insulin, proinsulin and glucagon extracted from their pancreases. Proinsulin represented the same proportion of total immunoreactive insulin in both types of rats. In the radioimmunoassays, the radioreceptorassays and the bioassays, insulin, proinsulin and glucagon from obese rats were indistinguishable from insulin, proinsulin and glucagon from lean rats. It is concluded that the pancreatic hormones of obese (“fatty”) rats possess the same immunoreactivity and biological potency as those of nonobese rats. This excludes the possibility that some alteration in the biological properties of pancreas insulin and/or glucagon of fatty rats could explain the metabolic abnormalities observed in this type of obesity.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Diabetologia 12 (1976), S. 83-100 
    ISSN: 1432-0428
    Keywords: Insulin ; glucagon ; polypeptide hormones ; receptors ; plasma membrane ; isolated liver cells ; isolated fat cells ; liver membranes ; fat cell membranes ; cardiac membranes ; adenylate cyclase ; monoiodoinsulin ; monoiodoglucagon ; 125I-insulin binding ; 125I-glucagon binding ; radioreceptorassay ; structure-function relationships ; modified insulins ; obese hyperglycémic (ob/ob) mouse ; obesity ; receptor defect ; insulin resistance ; insulin-dextran-ferritin ; visualization of binding sites
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
  • 3
    Electronic Resource
    Electronic Resource
    Springer
    Diabetologia 13 (1977), S. 219-228 
    ISSN: 1432-0428
    Keywords: Insulin ; glucagon ; binding sites ; receptors ; liver plasma membrane ; hepatocyte ; erythrocyte ; chicken ; rat
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Specific binding of chicken and porcine insulin was demonstrated in isolated chicken hepatocytes, chicken liver plasma membranes and chicken erythrocytes. In the liver, the binding reaction was characterized by a sensitivity and an apparent affinity which were similar to those observed in rat liver and, in contrast, by a decreased number of binding sites. In chicken liver, there were about 5 times fewer binding sites per mg of membrane protein or per unit of cell surface area than in rat liver. In chicken erythrocytes, the number of insulin binding sites per cell was even lower than in chicken hepatocytes. This decreased insulin binding was not accounted for by a faster insulin degradation in chicken tissues. Glucagon binding sites also appeared to be less numerous in chicken than in rat liver, at least at low glucagon concentration; however, the decrease in maximal binding capacity in chicken liver involved insulin and not glucagon binding. That chicken cells are equipped with insulin receptors which are less numerous than in mammalian cells may explain, partly at least, the physiological state of insulin resistance observed in the chicken.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...