Production of peptide antisera specific for mouse and rat proinsulin C-peptide 2

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Standard

Production of peptide antisera specific for mouse and rat proinsulin C-peptide 2. / Blume, N; Madsen, O D; Kofod, Hans; Dyrberg, T.

I: Biomedica Biochimica Acta, Bind 49, Nr. 12, 1990, s. 1247-51.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Harvard

Blume, N, Madsen, OD, Kofod, H & Dyrberg, T 1990, 'Production of peptide antisera specific for mouse and rat proinsulin C-peptide 2', Biomedica Biochimica Acta, bind 49, nr. 12, s. 1247-51.

APA

Blume, N., Madsen, O. D., Kofod, H., & Dyrberg, T. (1990). Production of peptide antisera specific for mouse and rat proinsulin C-peptide 2. Biomedica Biochimica Acta, 49(12), 1247-51.

Vancouver

Blume N, Madsen OD, Kofod H, Dyrberg T. Production of peptide antisera specific for mouse and rat proinsulin C-peptide 2. Biomedica Biochimica Acta. 1990;49(12):1247-51.

Author

Blume, N ; Madsen, O D ; Kofod, Hans ; Dyrberg, T. / Production of peptide antisera specific for mouse and rat proinsulin C-peptide 2. I: Biomedica Biochimica Acta. 1990 ; Bind 49, Nr. 12. s. 1247-51.

Bibtex

@article{91a4a879203948069b829f277b5ae233,
title = "Production of peptide antisera specific for mouse and rat proinsulin C-peptide 2",
abstract = "Mice and rats have two functional non-allelic insulin genes. By using a synthetic peptide representing a common sequence in mouse and rat C-peptide 2 as antigen, we have produced rabbit antisera specific for an epitope which is not present in mouse or rat C-peptide 1. Long-term immunization did not seem to increase the end point titre as tested in direct ELISA. The specificity of the antiserum was determined by competitive ELISA and histochemistry on pancreas sections. Only the synthetic C-peptide 2, but not the homologous synthetic C-peptide 1 from mouse and rat competed efficiently in ELISA for antibody binding to the immunizing antigen. Antisera to C-peptide 2, stained islet beta-cells on mouse and rat, but not monkey pancreas sections in immunocytochemical analysis. Preabsorption to the synthetic C-peptide 2, but not the synthetic mouse and rat C-peptide 1 abolished staining. In conclusion we have produced peptide antisera to an antigenic epitope which is unique to mouse and rat C-peptide 2. Antisera recognizing this epitope may be effective tools to study differential expression of the two insulin genes in mouse and rat.",
keywords = "Amino Acids, Animals, C-Peptide, Enzyme-Linked Immunosorbent Assay, Epitopes, Immune Sera, Immunohistochemistry, Mice, Peptides, Proinsulin, Rats, Sequence Alignment",
author = "N Blume and Madsen, {O D} and Hans Kofod and T Dyrberg",
year = "1990",
language = "English",
volume = "49",
pages = "1247--51",
journal = "Biomedica Biochimica Acta",
issn = "0232-766X",
publisher = "Akademie Verlag GMBH",
number = "12",

}

RIS

TY - JOUR

T1 - Production of peptide antisera specific for mouse and rat proinsulin C-peptide 2

AU - Blume, N

AU - Madsen, O D

AU - Kofod, Hans

AU - Dyrberg, T

PY - 1990

Y1 - 1990

N2 - Mice and rats have two functional non-allelic insulin genes. By using a synthetic peptide representing a common sequence in mouse and rat C-peptide 2 as antigen, we have produced rabbit antisera specific for an epitope which is not present in mouse or rat C-peptide 1. Long-term immunization did not seem to increase the end point titre as tested in direct ELISA. The specificity of the antiserum was determined by competitive ELISA and histochemistry on pancreas sections. Only the synthetic C-peptide 2, but not the homologous synthetic C-peptide 1 from mouse and rat competed efficiently in ELISA for antibody binding to the immunizing antigen. Antisera to C-peptide 2, stained islet beta-cells on mouse and rat, but not monkey pancreas sections in immunocytochemical analysis. Preabsorption to the synthetic C-peptide 2, but not the synthetic mouse and rat C-peptide 1 abolished staining. In conclusion we have produced peptide antisera to an antigenic epitope which is unique to mouse and rat C-peptide 2. Antisera recognizing this epitope may be effective tools to study differential expression of the two insulin genes in mouse and rat.

AB - Mice and rats have two functional non-allelic insulin genes. By using a synthetic peptide representing a common sequence in mouse and rat C-peptide 2 as antigen, we have produced rabbit antisera specific for an epitope which is not present in mouse or rat C-peptide 1. Long-term immunization did not seem to increase the end point titre as tested in direct ELISA. The specificity of the antiserum was determined by competitive ELISA and histochemistry on pancreas sections. Only the synthetic C-peptide 2, but not the homologous synthetic C-peptide 1 from mouse and rat competed efficiently in ELISA for antibody binding to the immunizing antigen. Antisera to C-peptide 2, stained islet beta-cells on mouse and rat, but not monkey pancreas sections in immunocytochemical analysis. Preabsorption to the synthetic C-peptide 2, but not the synthetic mouse and rat C-peptide 1 abolished staining. In conclusion we have produced peptide antisera to an antigenic epitope which is unique to mouse and rat C-peptide 2. Antisera recognizing this epitope may be effective tools to study differential expression of the two insulin genes in mouse and rat.

KW - Amino Acids

KW - Animals

KW - C-Peptide

KW - Enzyme-Linked Immunosorbent Assay

KW - Epitopes

KW - Immune Sera

KW - Immunohistochemistry

KW - Mice

KW - Peptides

KW - Proinsulin

KW - Rats

KW - Sequence Alignment

M3 - Journal article

C2 - 1711321

VL - 49

SP - 1247

EP - 1251

JO - Biomedica Biochimica Acta

JF - Biomedica Biochimica Acta

SN - 0232-766X

IS - 12

ER -

ID: 45574884