Functional improvement of antibody fragments using a novel phage coat protein III fusion system

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

Functional improvement of antibody fragments using a novel phage coat protein III fusion system. / Jensen, Kim Bak; Larsen, Martin; Pedersen, Jesper Søndergaard; Christensen, Peter Astrup; Alvarez-Vallina, Luis; Goletz, Steffen; Clark, Brian F C; Kristensen, Peter.

In: Molecular Cell Biology Research Communications, Vol. 298, No. 4, 08.11.2002, p. 566-73.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Jensen, KB, Larsen, M, Pedersen, JS, Christensen, PA, Alvarez-Vallina, L, Goletz, S, Clark, BFC & Kristensen, P 2002, 'Functional improvement of antibody fragments using a novel phage coat protein III fusion system', Molecular Cell Biology Research Communications, vol. 298, no. 4, pp. 566-73.

APA

Jensen, K. B., Larsen, M., Pedersen, J. S., Christensen, P. A., Alvarez-Vallina, L., Goletz, S., Clark, B. F. C., & Kristensen, P. (2002). Functional improvement of antibody fragments using a novel phage coat protein III fusion system. Molecular Cell Biology Research Communications, 298(4), 566-73.

Vancouver

Jensen KB, Larsen M, Pedersen JS, Christensen PA, Alvarez-Vallina L, Goletz S et al. Functional improvement of antibody fragments using a novel phage coat protein III fusion system. Molecular Cell Biology Research Communications. 2002 Nov 8;298(4):566-73.

Author

Jensen, Kim Bak ; Larsen, Martin ; Pedersen, Jesper Søndergaard ; Christensen, Peter Astrup ; Alvarez-Vallina, Luis ; Goletz, Steffen ; Clark, Brian F C ; Kristensen, Peter. / Functional improvement of antibody fragments using a novel phage coat protein III fusion system. In: Molecular Cell Biology Research Communications. 2002 ; Vol. 298, No. 4. pp. 566-73.

Bibtex

@article{9a28225b7650451d861874a00d71ef8e,
title = "Functional improvement of antibody fragments using a novel phage coat protein III fusion system",
abstract = "Functional expressions of proteins often depend on the presence of host specific factors. Frequently recombinant expression strategies of proteins in foreign hosts, such as bacteria, have been associated with poor yields or significant loss of functionality. Improvements in the performance of heterologous expression systems will benefit present-day quests in structural and functional genomics where high amounts of active protein are required. One example, which has been the subject of considerable interest, is recombinant antibodies or fragments thereof as expressions of these in bacteria constitute an easy and inexpensive method compared to hybridoma cultures. Such approaches have, however, often suffered from low yields and poor functionality. A general method is described here which enables expressions of functional antibody fragments when fused to the amino-terminal domain(s) of the filamentous phage coat protein III. Furthermore, it will be shown that the observed effect is neither due to improved stability nor increased avidity.",
keywords = "Base Sequence, Capsid Proteins/chemistry, Chromatography, Gel, DNA Primers, Enzyme-Linked Immunosorbent Assay, Immunoglobulin Fragments/immunology, Inovirus/immunology, Recombinant Fusion Proteins/chemistry",
author = "Jensen, {Kim Bak} and Martin Larsen and Pedersen, {Jesper S{\o}ndergaard} and Christensen, {Peter Astrup} and Luis Alvarez-Vallina and Steffen Goletz and Clark, {Brian F C} and Peter Kristensen",
year = "2002",
month = nov,
day = "8",
language = "English",
volume = "298",
pages = "566--73",
journal = "Biochemical and Biophysical Research Communications",
issn = "0006-291X",
publisher = "Elsevier",
number = "4",

}

RIS

TY - JOUR

T1 - Functional improvement of antibody fragments using a novel phage coat protein III fusion system

AU - Jensen, Kim Bak

AU - Larsen, Martin

AU - Pedersen, Jesper Søndergaard

AU - Christensen, Peter Astrup

AU - Alvarez-Vallina, Luis

AU - Goletz, Steffen

AU - Clark, Brian F C

AU - Kristensen, Peter

PY - 2002/11/8

Y1 - 2002/11/8

N2 - Functional expressions of proteins often depend on the presence of host specific factors. Frequently recombinant expression strategies of proteins in foreign hosts, such as bacteria, have been associated with poor yields or significant loss of functionality. Improvements in the performance of heterologous expression systems will benefit present-day quests in structural and functional genomics where high amounts of active protein are required. One example, which has been the subject of considerable interest, is recombinant antibodies or fragments thereof as expressions of these in bacteria constitute an easy and inexpensive method compared to hybridoma cultures. Such approaches have, however, often suffered from low yields and poor functionality. A general method is described here which enables expressions of functional antibody fragments when fused to the amino-terminal domain(s) of the filamentous phage coat protein III. Furthermore, it will be shown that the observed effect is neither due to improved stability nor increased avidity.

AB - Functional expressions of proteins often depend on the presence of host specific factors. Frequently recombinant expression strategies of proteins in foreign hosts, such as bacteria, have been associated with poor yields or significant loss of functionality. Improvements in the performance of heterologous expression systems will benefit present-day quests in structural and functional genomics where high amounts of active protein are required. One example, which has been the subject of considerable interest, is recombinant antibodies or fragments thereof as expressions of these in bacteria constitute an easy and inexpensive method compared to hybridoma cultures. Such approaches have, however, often suffered from low yields and poor functionality. A general method is described here which enables expressions of functional antibody fragments when fused to the amino-terminal domain(s) of the filamentous phage coat protein III. Furthermore, it will be shown that the observed effect is neither due to improved stability nor increased avidity.

KW - Base Sequence

KW - Capsid Proteins/chemistry

KW - Chromatography, Gel

KW - DNA Primers

KW - Enzyme-Linked Immunosorbent Assay

KW - Immunoglobulin Fragments/immunology

KW - Inovirus/immunology

KW - Recombinant Fusion Proteins/chemistry

M3 - Journal article

C2 - 12408989

VL - 298

SP - 566

EP - 573

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

SN - 0006-291X

IS - 4

ER -

ID: 200572782