Radio-immunoassays for glucagon-like peptides 1 and 2 (GLP-1 and GLP-2)

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Radio-immunoassays for glucagon-like peptides 1 and 2 (GLP-1 and GLP-2). / Orskov, C; Holst, J J.

In: Scandinavian Journal of Clinical and Laboratory Investigation. Supplement, Vol. 47, No. 2, 04.1987, p. 165-74.

Research output: Contribution to journalJournal articleResearchpeer-review

Harvard

Orskov, C & Holst, JJ 1987, 'Radio-immunoassays for glucagon-like peptides 1 and 2 (GLP-1 and GLP-2)', Scandinavian Journal of Clinical and Laboratory Investigation. Supplement, vol. 47, no. 2, pp. 165-74.

APA

Orskov, C., & Holst, J. J. (1987). Radio-immunoassays for glucagon-like peptides 1 and 2 (GLP-1 and GLP-2). Scandinavian Journal of Clinical and Laboratory Investigation. Supplement, 47(2), 165-74.

Vancouver

Orskov C, Holst JJ. Radio-immunoassays for glucagon-like peptides 1 and 2 (GLP-1 and GLP-2). Scandinavian Journal of Clinical and Laboratory Investigation. Supplement. 1987 Apr;47(2):165-74.

Author

Orskov, C ; Holst, J J. / Radio-immunoassays for glucagon-like peptides 1 and 2 (GLP-1 and GLP-2). In: Scandinavian Journal of Clinical and Laboratory Investigation. Supplement. 1987 ; Vol. 47, No. 2. pp. 165-74.

Bibtex

@article{79402eff0f5f47a6afa19ef0c7cec474,
title = "Radio-immunoassays for glucagon-like peptides 1 and 2 (GLP-1 and GLP-2)",
abstract = "Gene-sequencing studies have shown that the glucagon precursor contains two additional glucagon-like sequences, the so-called glucagon-like peptides 1 and 2 (GLP-1 and GLP-2). We developed radio-immunoassays against synthetic peptides corresponding to these sequences. Antisera were raised in rabbits after carbodiimide conjugation of peptides to BSA. The selected antisera showed neither mutual cross-reactivity nor cross-reacted with any other peptide of the glucagon family. Trypsin digestion experiments showed that both antisera were directed against the C-terminus of the antigen peptides. Labelling was performed with chloramine T, and separation with plasma-coated charcoal. The detection limit was 7 and 25 pmol/l for GLP-1 and GLP-2. Accurate measurement of both peptides in plasma required extraction. Optimum recovery was obtained with ethanol at 75{\%} (final concentration). The concentrations measured in fasting plasma from 10 normal subjects were 107 +/- 7 pmol/l and 151 +/- 14 pmol/l for GLP-1 and GLP-2, respectively. After a mixed meal the concentrations rose slowly for 2 h reaching 145 +/- 13 and 225 +/- 15 pmol/l.",
keywords = "Animals, Chromatography, Gel, Glucagon-Like Peptide 1, Glucagon-Like Peptide 2, Humans, Hydrogen-Ion Concentration, Immune Sera, Peptides/blood, Rabbits, Radioimmunoassay/methods",
author = "C Orskov and Holst, {J J}",
year = "1987",
month = "4",
language = "English",
volume = "47",
pages = "165--74",
journal = "Scandinavian Journal of Clinical and Laboratory Investigation. Supplement",
issn = "0085-591X",
publisher = "Taylor & Francis",
number = "2",

}

RIS

TY - JOUR

T1 - Radio-immunoassays for glucagon-like peptides 1 and 2 (GLP-1 and GLP-2)

AU - Orskov, C

AU - Holst, J J

PY - 1987/4

Y1 - 1987/4

N2 - Gene-sequencing studies have shown that the glucagon precursor contains two additional glucagon-like sequences, the so-called glucagon-like peptides 1 and 2 (GLP-1 and GLP-2). We developed radio-immunoassays against synthetic peptides corresponding to these sequences. Antisera were raised in rabbits after carbodiimide conjugation of peptides to BSA. The selected antisera showed neither mutual cross-reactivity nor cross-reacted with any other peptide of the glucagon family. Trypsin digestion experiments showed that both antisera were directed against the C-terminus of the antigen peptides. Labelling was performed with chloramine T, and separation with plasma-coated charcoal. The detection limit was 7 and 25 pmol/l for GLP-1 and GLP-2. Accurate measurement of both peptides in plasma required extraction. Optimum recovery was obtained with ethanol at 75% (final concentration). The concentrations measured in fasting plasma from 10 normal subjects were 107 +/- 7 pmol/l and 151 +/- 14 pmol/l for GLP-1 and GLP-2, respectively. After a mixed meal the concentrations rose slowly for 2 h reaching 145 +/- 13 and 225 +/- 15 pmol/l.

AB - Gene-sequencing studies have shown that the glucagon precursor contains two additional glucagon-like sequences, the so-called glucagon-like peptides 1 and 2 (GLP-1 and GLP-2). We developed radio-immunoassays against synthetic peptides corresponding to these sequences. Antisera were raised in rabbits after carbodiimide conjugation of peptides to BSA. The selected antisera showed neither mutual cross-reactivity nor cross-reacted with any other peptide of the glucagon family. Trypsin digestion experiments showed that both antisera were directed against the C-terminus of the antigen peptides. Labelling was performed with chloramine T, and separation with plasma-coated charcoal. The detection limit was 7 and 25 pmol/l for GLP-1 and GLP-2. Accurate measurement of both peptides in plasma required extraction. Optimum recovery was obtained with ethanol at 75% (final concentration). The concentrations measured in fasting plasma from 10 normal subjects were 107 +/- 7 pmol/l and 151 +/- 14 pmol/l for GLP-1 and GLP-2, respectively. After a mixed meal the concentrations rose slowly for 2 h reaching 145 +/- 13 and 225 +/- 15 pmol/l.

KW - Animals

KW - Chromatography, Gel

KW - Glucagon-Like Peptide 1

KW - Glucagon-Like Peptide 2

KW - Humans

KW - Hydrogen-Ion Concentration

KW - Immune Sera

KW - Peptides/blood

KW - Rabbits

KW - Radioimmunoassay/methods

M3 - Journal article

VL - 47

SP - 165

EP - 174

JO - Scandinavian Journal of Clinical and Laboratory Investigation. Supplement

JF - Scandinavian Journal of Clinical and Laboratory Investigation. Supplement

SN - 0085-591X

IS - 2

ER -

ID: 194816936