Untractable Hypoglycemia in an Infant: Studies on Pancreas Insulin and Glucagon

Rançon, F; Laburthe, Marc; Rosselin, G; Freychet, P

doi:10.1055/s-0028-1093820

Cited by 4 publications

(2 citation statements)

References 8 publications

(10 reference statements)

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“…Highly or partially purified plasma membranes from the liver [11,12,[17][18][19][20][21][22][23][24][25][26][27][28], adipocyte [24,27,29] and myocardium [30] were used in the studies presented here. There is a distinct value in using the most purified preparation of plasma membrane available in binding studies.…”

Section: Receptor Preparationsmentioning

confidence: 99%

Interactions of polypeptide hormones with cell membrane specific receptors: Studies with insulin and glucagon

Freychet

1976

Diabetologia

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122

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Section: Receptor Preparationsmentioning

confidence: 99%

Interactions of polypeptide hormones with cell membrane specific receptors: Studies with insulin and glucagon

Freychet

1976

Diabetologia

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122

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“…Insulin and glucagon were extracted from pooled pancreases according to Kenny [9], with modifications described elsewhere [10]. Powdered pancreatic extracts (100 mg) were dissolved in 3 M acetic acid and submitted to gel filtration on a 2.5 • 140 cm column of Sephadex G-50 (Pharmacia) equilibrated and eluted with 1 M acetic acid, pH 2.4, at a flow rate of 0.3 ml/min/cm 2.…”

Section: Extraction and Fractionation Of The Hormonesmentioning

confidence: 99%

Glucagon and insulin from lean rats and genetically obese fatty rats: Studies by radioimmunoassay, radioreceptorassay and bioassay

et al. 1975

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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 of 125I-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 of 125I-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.

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Radioreceptorassays for Glucagon

Holst¹

1983

Glucagon I

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Untractable Hypoglycemia in an Infant: Studies on Pancreas Insulin and Glucagon

Abstract: Herring: Insulin-resistant diabetes associated with increased endogenous plasma insulin followed by complete remission.

Cited by 4 publications

References 8 publications

Interactions of polypeptide hormones with cell membrane specific receptors: Studies with insulin and glucagon

Interactions of polypeptide hormones with cell membrane specific receptors: Studies with insulin and glucagon

Glucagon and insulin from lean rats and genetically obese fatty rats: Studies by radioimmunoassay, radioreceptorassay and bioassay

Radioreceptorassays for Glucagon

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