The use of antibodies for characterization and quantification of a recombinant protein

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Standard

The use of antibodies for characterization and quantification of a recombinant protein. / Sabater, Margarita; Heilmann, Susanne; Frøkiær, Hanne; Biedermann, Kirsten; Emborg, Claus.

I: Annals of the New York Academy of Sciences, Bind 782, 1996, s. 462-477.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Harvard

Sabater, M, Heilmann, S, Frøkiær, H, Biedermann, K & Emborg, C 1996, 'The use of antibodies for characterization and quantification of a recombinant protein', Annals of the New York Academy of Sciences, bind 782, s. 462-477. https://doi.org/10.1111/j.1749-6632.1996.tb40584.x

APA

Sabater, M., Heilmann, S., Frøkiær, H., Biedermann, K., & Emborg, C. (1996). The use of antibodies for characterization and quantification of a recombinant protein. Annals of the New York Academy of Sciences, 782, 462-477. https://doi.org/10.1111/j.1749-6632.1996.tb40584.x

Vancouver

Sabater M, Heilmann S, Frøkiær H, Biedermann K, Emborg C. The use of antibodies for characterization and quantification of a recombinant protein. Annals of the New York Academy of Sciences. 1996;782:462-477. https://doi.org/10.1111/j.1749-6632.1996.tb40584.x

Author

Sabater, Margarita ; Heilmann, Susanne ; Frøkiær, Hanne ; Biedermann, Kirsten ; Emborg, Claus. / The use of antibodies for characterization and quantification of a recombinant protein. I: Annals of the New York Academy of Sciences. 1996 ; Bind 782. s. 462-477.

Bibtex

@article{e532f324b5034328bdf5ff2ebcf956a5,
title = "The use of antibodies for characterization and quantification of a recombinant protein",
abstract = "In this study, we characterized proteinase A secreted by recombinant Saccharomyces cerevisiae bearing a multicopy plasmid containing the encoding gene (PEP4). Polyclonal and monoclonal antibodies were raised to study the product heterogeneity. Characterization of proteinase A was performed by immunoelectrophoresis and immunoblotting techniques. None of the monoclonal antibodies raised against proteinase A was found to react with the glycosyl side chains; thus cross-reaction with other glycosylated proteins (e.g. carboxypeptidase Y) was very low. This study allowed us to develop an ELISA method for the quantification of proteinase A in culture supernatants as well as the evaluation of monoclonal antibodies for their use in immunoaffinity chromatography.",
author = "Margarita Sabater and Susanne Heilmann and Hanne Fr{\o}ki{\ae}r and Kirsten Biedermann and Claus Emborg",
year = "1996",
doi = "10.1111/j.1749-6632.1996.tb40584.x",
language = "English",
volume = "782",
pages = "462--477",
journal = "Annals of The Lyceum of Natural History of New York",
issn = "0077-8923",
publisher = "Wiley-Blackwell",

}

RIS

TY - JOUR

T1 - The use of antibodies for characterization and quantification of a recombinant protein

AU - Sabater, Margarita

AU - Heilmann, Susanne

AU - Frøkiær, Hanne

AU - Biedermann, Kirsten

AU - Emborg, Claus

PY - 1996

Y1 - 1996

N2 - In this study, we characterized proteinase A secreted by recombinant Saccharomyces cerevisiae bearing a multicopy plasmid containing the encoding gene (PEP4). Polyclonal and monoclonal antibodies were raised to study the product heterogeneity. Characterization of proteinase A was performed by immunoelectrophoresis and immunoblotting techniques. None of the monoclonal antibodies raised against proteinase A was found to react with the glycosyl side chains; thus cross-reaction with other glycosylated proteins (e.g. carboxypeptidase Y) was very low. This study allowed us to develop an ELISA method for the quantification of proteinase A in culture supernatants as well as the evaluation of monoclonal antibodies for their use in immunoaffinity chromatography.

AB - In this study, we characterized proteinase A secreted by recombinant Saccharomyces cerevisiae bearing a multicopy plasmid containing the encoding gene (PEP4). Polyclonal and monoclonal antibodies were raised to study the product heterogeneity. Characterization of proteinase A was performed by immunoelectrophoresis and immunoblotting techniques. None of the monoclonal antibodies raised against proteinase A was found to react with the glycosyl side chains; thus cross-reaction with other glycosylated proteins (e.g. carboxypeptidase Y) was very low. This study allowed us to develop an ELISA method for the quantification of proteinase A in culture supernatants as well as the evaluation of monoclonal antibodies for their use in immunoaffinity chromatography.

UR - http://www.scopus.com/inward/record.url?scp=0030004745&partnerID=8YFLogxK

U2 - 10.1111/j.1749-6632.1996.tb40584.x

DO - 10.1111/j.1749-6632.1996.tb40584.x

M3 - Journal article

C2 - 8659917

AN - SCOPUS:0030004745

VL - 782

SP - 462

EP - 477

JO - Annals of The Lyceum of Natural History of New York

JF - Annals of The Lyceum of Natural History of New York

SN - 0077-8923

ER -

ID: 331794754