Patent EP0338745A1 successfully refreshed from Google Patents.
EP0338745A1
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EP
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Method for producing recombinant DNA proteins
Assignee: Celltech R&D Ltd
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Filing: 1989-04-17
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Granted: —
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Expires: 2009-04-17
Abstract
Abstract The present invention provides a method for producing Fv fragments comprising: transforming a eukaryotic host cell with a eukaryotic expression vector comprising an operon having a DNA sequence which encodes the variable domain only of an antibody light or heavy chain, culturing the transformed host cell under conditions which cause the protein encoded by the DNA sequence to be synthesised; and collecting the synthesised protein.
Inventors
- 👤 Raymond John Owens
- 👤 Gregory Paul Winter
- 👤 Lutz Riechmann
- 👤 Geoffrey Thomas Yarranton
- 👤 Mark William Bodmer
Bibliographic Details
Application Number
—
Jurisdiction
EP
Data Source
google_patents
Last Synchronized
2026-11-03 18:26
CPC Classifications
C; C07; C07K; C07K16/00; C07K16/40; C07K2317/00; C07K2317/20; C07K2317/24; C07K2317/50; C07K2317/56
Claims Analysis
Total Claims: 11
Claim 1
Independent Claim
61 words
A method for producing Fv fragments comprising: transforming a eukaryotic host cell with a eukaryotic expression vector comprising an operon having a DNA sequence which encodes the variable domain only of an antibody light or heavy chain, culturing the transformed host cell under conditions which cause the protein encoded by the DNA sequence to be synthesised; and collecting the synthesised protein.
Claim 2
Independent Claim
61 words
A method for producing Fv fragments comprising: transforming a eukaryotic host cell with a eukaryotic expression vector comprising an operon having a DNA sequence which encodes the variable domain only of an antibody light or heavy chain, culturing the transformed host cell under conditions which cause the protein encoded by the DNA sequence to be synthesised; and collecting the synthesised protein.
Claim 3
Dependent Claim
33 words
The method of claim 1, wherein the chains of the Fv fragment are secreted and correctly assembled by the host cell such that fully functional Fv fragments are produced in the culture supernatant.
Claim 4
Dependent Claim
38 words
The method of claim 1 or claim 2, wherein the host cell is also transformed with a second eukaryotic expression vector comprising an operon having a DNA sequence encoding a complementary heavy or light chain variable domain respectively.
Claim 5
Dependent Claim
31 words
The method of claim 1 or claim 2, wherein the first expression vector has a second operon comprising a DNA sequence encoding a complementary heavy or light chain variable domain respectively.
Claim 6
Dependent Claim
36 words
The method of claim 3 or claim 4, wherein the or each variable domain is expressed as a fusion protein having an effector protein, such as an enzyme, ligand or toxin, fused to its C-terminal end.
Claim 7
Independent Claim
41 words
The method of any one of claims 3 to 5, wherein the or each DNA coding sequence may be altered towards its 3′ end so that one or more cysteine residues are produced towards the C-terminal end of each variable domain.
Claim 8
Independent Claim
62 words
The method of any one of claims 3 to 5, wherein the Fv fragment is stabilised by use of a vector having in the operon a first DNA sequence encoding a first variable domain and a second DNA sequence encoding a second variable domain, the first and second sequences being linked by a third DNA sequence which encodes a joining peptide sequence.
Claim 9
Independent Claim
19 words
The method of any one of claims 1 to 7, wherein the coding sequence(s) are derived from monoclonal antibodies.
Claim 10
Dependent Claim
32 words
An Fv structure wherein one or both of the domains comprises a fusion protein having the variable domain at its N-terminal end and an enzyme, ligand or toxin at its C-terminal end.
Claim 11
Dependent Claim
32 words
An Fv structure wherein one or both of the domains comprises a fusion protein having the variable domain at its N-terminal end and an enzyme, ligand or toxin at its C-terminal end.
References Cited (Backward Citations)
WO1988001649A1
Cited
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