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Immunoglobulin half-molecules and process for producing hybrid antibodies

Assignee: Dade Behring Inc
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Filing: 1983-10-04
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Granted: 1984-09-11
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Expires: 2003-10-04
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Abstract

Abstract A process for preparing covalent hybrid antibodies is provided. These antibodies are obtained by the ordered covalent hybridization of intact immunoglobulin molecules. The generation of half-molecules from different IgG antibodies by reductive or S-sulfonation selective cleavage is followed by the ordered association of the different half-molecules. The pure covalent hybrid antibodies as new substances are also provided along with IgG half-molecules.

Inventors

  • 👤 Karen Auditore-Hargreaves

Bibliographic Details

Application Number —
Jurisdiction US
Data Source google_patents
Last Synchronized 2026-10-24 13:16
CPC Classifications
G; G01; G01N; G01N33/00; G01N33/48; G01N33/50; G01N33/53; G01N33/531; A; A61; A61K; A61K47/00; A61K47/50; A61K47/51; A61K47/68; G01N33/577; G01N33/68; G01N33/6854; G01N33/94; Y; Y10; Y10S; Y10S530/00; Y10S530/827; Y10S530/829; Y10S530/83; Y10S530/866

Claims Analysis

Total Claims: 14
Claim 1
Independent Claim 60 words
A substantially pure covalent hybrid antibody consisting essentially of two different heavy chain-light chain half-molecules, wherein the first of said half-molecules provides a binding site for a first antigen and the second of said half-molecules provides a chemically different binding site for the first or a second antigen; and wherein said half-molecules are bonded to each other through disulfide linkage.
Claim 2
Dependent Claim 60 words
A substantially pure covalent hybrid antibody consisting essentially of two different heavy chain-light chain half-molecules, wherein the first of said half-molecules provides a binding site for a first antigen and the second of said half-molecules provides a chemically different binding site for the first or a second antigen; and wherein said half-molecules are bonded to each other through disulfide linkage.
Claim 3
Dependent Claim 21 words
The covalent hybrid antibody of claim 1 wherein the first and second half-molecules provide chemically different binding sites for different antigens.
Claim 4
Dependent Claim 29 words
The covalent hybrid antibody of claim 2 wherein the first half-molecule provides a binding site for an analyte and the second half-molecule provides a binding site for an indicator.
Claim 5
Dependent Claim 32 words
The covalent hybrid antibody of claim 3 wherein the analyte is selected from the group consisting of protein, hormone, drug, vitamin, enzyme, antibody, polysaccharide, bacterium, protozoa, fungi, virus, cell and tissue antigens.
Claim 6
Dependent Claim 21 words
The covalent hybrid antibody of claim 3 wherein the indicator is selected from the group consisting of enzyme and aggregating substance.
Claim 7
Dependent Claim 96 words
A process for preparing covalent hybrid antibodies comprising the steps of: (A) selectively cleaving a first immunoglobulin molecule which is an antibody to a first antigen into its heavy chain-light chain half-molecules by sulfitolysis of the inter-heavy chain disulfide linkage to produce S-sulfonated half-molecules; (B) selectively cleaving a second immunoglobulin molecule which is an antibody to the first or a second antigen into its heavy chain-light chain half-molecules by reduction of the inter-heavy chain disulfide linkage to produce reduced half-molecules; and (C) combining the S-sulfonated half-molecules from step (A) with the reduced half-molecules from step (B).
Claim 8
Dependent Claim 96 words
A process for preparing covalent hybrid antibodies comprising the steps of: (A) selectively cleaving a first immunoglobulin molecule which is an antibody to a first antigen into its heavy chain-light chain half-molecules by sulfitolysis of the inter-heavy chain disulfide linkage to produce S-sulfonated half-molecules; (B) selectively cleaving a second immunoglobulin molecule which is an antibody to the first or a second antigen into its heavy chain-light chain half-molecules by reduction of the inter-heavy chain disulfide linkage to produce reduced half-molecules; and (C) combining the S-sulfonated half-molecules from step (A) with the reduced half-molecules from step (B).
Claim 9
Dependent Claim 19 words
The process of claim 6 wherein the reduced half-molecules are produced by reduction of the inter-heavy chain disulfide linkage.
Claim 10
Dependent Claim 22 words
The process of claim 6 wherein the reduced half-molecules are produced by sulfitolysis of the inter-heavy chain disulfide linkage followed by reduction.
Claim 11
Dependent Claim 36 words
The process of claim 8 wherein the sulfitolysis reaction comprises the steps of: (A) mixing an immunoglobulin molecule with sodium sulfite and 5,5'-dithiobis(2-nitrobenzoic acid); (B) incubating in a nonoxidizing atmosphere; and (C) separating the protein products.
Claim 12
Dependent Claim 21 words
The process of claim 7 wherein the reduced half-molecules are produced by reduction of immunoglobulin molecule bound to an immobilized receptor.
Claim 13
Dependent Claim 14 words
The process of claim 10 wherein the receptor is antigen bonded to a support.
Claim 14
Dependent Claim 15 words
The process of claim 10 wherein the receptor is Protein A bonded to a support.

References Cited (Backward Citations)

US3995018A Cited
US3995018B1 Cited
US3995018B2 Cited
US4059571A Cited
US4160763A Cited
US4302384A Cited
US4360457A Cited
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USPTO Annuity & Maintenance Windows

Annuity Stage Window Opens Payment Deadline Surcharge Period Until Estimated Fee Status
3.5 Years (Year 4) 1987-09-11 1988-03-12 1988-09-11 $2000.00 Window Closed / Lapsed
7.5 Years (Year 8) 1991-09-11 1992-03-12 1992-09-11 $3760.00 Window Closed / Lapsed
11.5 Years (Year 12) 1995-09-11 1996-03-12 1996-09-11 $7700.00 Window Closed / Lapsed

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