US4708929A
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Methods for protein binding enzyme complementation assays
Assignee: Roche Diagnostics Corp
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Filing: 1985-04-08
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Granted: 1987-11-24
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Expires: 2005-04-08
Abstract
Abstract This invention relates to improved methods and novel compositions for enzyme complementation assays for qualitative and quantitative determination of a suspected analyte in a sample. The use of enzyme-acceptor and enzyme-donor polypeptides prepared by recombinant DNA techniques or chemical polypeptide synthesis techniques which are capable of interacting to form an active enzyme complex having catalytic activity characteristic of beta -galactosidase is described. Both homogeneous and heterogeneous assays utilizing these polypeptides are described.
Inventors
- 👤 Daniel R. Henderson
Bibliographic Details
Application Number
—
Jurisdiction
US
Data Source
google_patents
Last Synchronized
2026-11-07 21:57
CPC Classifications
C; C07; C07K; C07K14/00; C07K14/005; C07K14/435; C07K14/575; C07K14/59; C12; C12N; C12N15/00; C12N15/09; C12N15/11; C12N15/62; C12N9/00; C12N9/14; C12N9/24; C12N9/2402; C12N9/2468; C12N9/2471; C12Y; C12Y302/00; C12Y302/01; C12Y302/01023; G; G01; G01N; G01N33/00; G01N33/48; G01N33/50; G01N33/53; G01N33/531; G01N33/532; G01N33/535; C07K2319/00; C07K2319/01; C07K2319/02; C07K2319/35; C07K2319/40; C07K2319/61; C07K2319/70; C07K2319/74; C07K2319/75; C12N2730/00; C12N2730/00011; C12N2730/10011; C12N2730/10111; C12N2730/10122; Y; Y10; Y10S; Y10S435/00; Y10S435/975
Claims Analysis
Total Claims: 5
Claim 1
Independent Claim
269 words
An enzyme assay method for determining the amount of a suspected analyte in a sample which comprises the steps of: (a) Forming a reaction mixture by combining in a medium (1) sample; (2) an enzyme-donor polypeptide conjugate; (3) an analyte-binding protein specific for said analyte; and (4) an enzyme-acceptor polypeptide consisting essentially of a fragment of β-galactosidase, wherein said enzyme-donor polypeptide conjugate and enzyme acceptor polypeptide are prepared by recombinant DNA techniques or chemical polypeptide synthesis techniques, wherein said enzyme-donor polypeptide is characterized by forming with said enzyme-acceptor polypeptide, an active enzyme complex having β-galactosidase activity in the absence of analyte-binding protein binding to said conjugate, said enzyme donor polypeptide conjugate being further characterized by having substantially as the internal amino acid sequence, amino acids 6-51 of β-galactosidase, having one cysteine, with analyte joined to said one cysteine, and having an N-terminal sequence and a C-terminal sequence or having substantially as the amino acid sequence amino acids 7-44 of β-galactosidase, having one cysteine with analyte joined to said one cysteine and having at least an N-terminal sequence and (5) a substrate capable of reacting with said active enzyme complex, such that the rate of conversion by said active enzyme complex can be monitored; and wherein said enzyme-donor conjugate is capable of competitively binding to the analyte-binding protein inhibiting the formation of active enzyme complex; (b) measuring the rate of conversion of substrate in the reaction mixture; and (c) determining the amount of analyte in the sample by comparing the rate of conversion of substrate to a rate of conversion of substrate obtained using a known concentration of the analyte.
Claim 2
Dependent Claim
269 words
An enzyme assay method for determining the amount of a suspected analyte in a sample which comprises the steps of: (a) Forming a reaction mixture by combining in a medium (1) sample; (2) an enzyme-donor polypeptide conjugate; (3) an analyte-binding protein specific for said analyte; and (4) an enzyme-acceptor polypeptide consisting essentially of a fragment of β-galactosidase, wherein said enzyme-donor polypeptide conjugate and enzyme acceptor polypeptide are prepared by recombinant DNA techniques or chemical polypeptide synthesis techniques, wherein said enzyme-donor polypeptide is characterized by forming with said enzyme-acceptor polypeptide, an active enzyme complex having β-galactosidase activity in the absence of analyte-binding protein binding to said conjugate, said enzyme donor polypeptide conjugate being further characterized by having substantially as the internal amino acid sequence, amino acids 6-51 of β-galactosidase, having one cysteine, with analyte joined to said one cysteine, and having an N-terminal sequence and a C-terminal sequence or having substantially as the amino acid sequence amino acids 7-44 of β-galactosidase, having one cysteine with analyte joined to said one cysteine and having at least an N-terminal sequence and (5) a substrate capable of reacting with said active enzyme complex, such that the rate of conversion by said active enzyme complex can be monitored; and wherein said enzyme-donor conjugate is capable of competitively binding to the analyte-binding protein inhibiting the formation of active enzyme complex; (b) measuring the rate of conversion of substrate in the reaction mixture; and (c) determining the amount of analyte in the sample by comparing the rate of conversion of substrate to a rate of conversion of substrate obtained using a known concentration of the analyte.
Claim 3
Dependent Claim
28 words
A method according to claim 1 wherein said one cysteine is at amino acid position 3, 20, 39, or 46, based on β-galactosidase numbering as in FIG. 15.
Claim 4
Dependent Claim
43 words
A method according to claim 1, wherein said one cysteine is in the N- or C-terminal sequence and said N-terminal sequence is of up to and including 27 amino acids and said C-terminal sequence is of up to and including 17 amino acids.
Claim 5
Independent Claim
153 words
A method according to any of claims 1, 2, or 3, wherein said N-terminal sequence has the sequence: ______________________________________
M D P S G N P Y G I D P T E S S P G N I D P R A S S N,
M D P S G D P R A S S N,
M D P R A S S N, or
C I T D;
______________________________________ and said C-terminal sequence has the sequence: ______________________________________
A Q P E W G L E S R S A G M P L E,
R S L N G L E S R S A G M P L E, or
R S L N G E L C G V K Y R T D A,
______________________________________ with the proviso that where said N-terminal or C-terminal sequence has said one cysteine, said internal amino acid sequence lacks said cysteine.
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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) | 1990-11-23 | 1991-05-25 | 1991-11-24 | $2000.00 | Window Closed / Lapsed |
| 7.5 Years (Year 8) | 1994-11-23 | 1995-05-25 | 1995-11-24 | $3760.00 | Window Closed / Lapsed |
| 11.5 Years (Year 12) | 1998-11-23 | 1999-05-25 | 1999-11-24 | $7700.00 | Window Closed / Lapsed |