You need JavaScript to view this

Quality control of insulin radioreceptor assay for human erythrocytes. Effect of ageing of mono-/sup 125/I-Tyr-A14-insulin preparation

Abstract

The quality control of insulin radioreceptor assay for human erythrocytes is based on the storage of erythrocyte preparations in Hepes buffer of pH 8.0, containing 10 g/l of albumin and 20 mmol/l of glucose. The change of erythrocytes into spherocytes and crenated cells reduces the apparent number of insulin receptors in a relatively constant way by less than 8% a week after 10 days of storage. At the same time the dissociation constants of the insulin-receptor complex increase rapidly. Thus the use of a preparation must be limited to controlling the determination of the insulin binding sites of erythrocytes, and not to the measurement of the affinities of the receptors. When mono-/sup 125/I-Tyr-A14-insulin gets old, a slow decrease in the insulin binding sites can be measured, but the dissociation constants of the insulin receptor complex are not affected.
Authors:
Marttinen, A; Pasternack, A; [1]  Koivula, T; Jokela, H; Lehtinen, M [2] 
  1. Tampere Univ. (Finland). Dept. of Clinical Sciences
  2. Tampere Univ. Central Hospital (Finland). Dept. of Clinical Chemistry
Publication Date:
Sep 01, 1984
Product Type:
Journal Article
Reference Number:
AIX-16-021071; EDB-85-097503
Resource Relation:
Journal Name: Scand. J. Clin. Lab. Invest.; (United Kingdom); Journal Volume: 44:5
Subject:
62 RADIOLOGY AND NUCLEAR MEDICINE; INSULIN; RADIORECEPTOR ASSAY; QUALITY CONTROL; ERYTHROCYTES; IODINE 125; LABELLED COMPOUNDS; MAN; PH VALUE; STORAGE; ANIMALS; BETA DECAY RADIOISOTOPES; BIOLOGICAL MATERIALS; BLOOD; BLOOD CELLS; BODY FLUIDS; CONTROL; DAYS LIVING RADIOISOTOPES; ELECTRON CAPTURE RADIOISOTOPES; HORMONES; INTERMEDIATE MASS NUCLEI; IODINE ISOTOPES; ISOTOPE APPLICATIONS; ISOTOPES; MAMMALS; MATERIALS; NUCLEI; ODD-EVEN NUCLEI; PEPTIDE HORMONES; PRIMATES; RADIOISOTOPES; TRACER TECHNIQUES; VERTEBRATES; 550601* - Medicine- Unsealed Radionuclides in Diagnostics
OSTI ID:
5754182
Country of Origin:
United Kingdom
Language:
English
Other Identifying Numbers:
Journal ID: CODEN: SJCLA
Submitting Site:
HEDB
Size:
Pages: 401-408
Announcement Date:
Feb 01, 1985

Citation Formats

Marttinen, A, Pasternack, A, Koivula, T, Jokela, H, and Lehtinen, M. Quality control of insulin radioreceptor assay for human erythrocytes. Effect of ageing of mono-/sup 125/I-Tyr-A14-insulin preparation. United Kingdom: N. p., 1984. Web. doi:10.3109/00365518409083828.
Marttinen, A, Pasternack, A, Koivula, T, Jokela, H, & Lehtinen, M. Quality control of insulin radioreceptor assay for human erythrocytes. Effect of ageing of mono-/sup 125/I-Tyr-A14-insulin preparation. United Kingdom. https://doi.org/10.3109/00365518409083828
Marttinen, A, Pasternack, A, Koivula, T, Jokela, H, and Lehtinen, M. 1984. "Quality control of insulin radioreceptor assay for human erythrocytes. Effect of ageing of mono-/sup 125/I-Tyr-A14-insulin preparation." United Kingdom. https://doi.org/10.3109/00365518409083828.
@misc{etde_5754182,
title = {Quality control of insulin radioreceptor assay for human erythrocytes. Effect of ageing of mono-/sup 125/I-Tyr-A14-insulin preparation}
author = {Marttinen, A, Pasternack, A, Koivula, T, Jokela, H, and Lehtinen, M}
abstractNote = {The quality control of insulin radioreceptor assay for human erythrocytes is based on the storage of erythrocyte preparations in Hepes buffer of pH 8.0, containing 10 g/l of albumin and 20 mmol/l of glucose. The change of erythrocytes into spherocytes and crenated cells reduces the apparent number of insulin receptors in a relatively constant way by less than 8% a week after 10 days of storage. At the same time the dissociation constants of the insulin-receptor complex increase rapidly. Thus the use of a preparation must be limited to controlling the determination of the insulin binding sites of erythrocytes, and not to the measurement of the affinities of the receptors. When mono-/sup 125/I-Tyr-A14-insulin gets old, a slow decrease in the insulin binding sites can be measured, but the dissociation constants of the insulin receptor complex are not affected.}
doi = {10.3109/00365518409083828}
journal = []
volume = {44:5}
journal type = {AC}
place = {United Kingdom}
year = {1984}
month = {Sep}
}