Chemistry: natural resins or derivatives; peptides or proteins; – Peptides of 3 to 100 amino acid residues – Chemical aftertreatment – e.g. – acylation – methylation – etc.
Patent
1988-07-01
1992-04-21
Naff, David M.
Chemistry: natural resins or derivatives; peptides or proteins;
Peptides of 3 to 100 amino acid residues
Chemical aftertreatment, e.g., acylation, methylation, etc.
435 74, 435183, 435199, 435207, 435 79, 530300, 530323, 530350, 530402, 530403, 530404, 530405, 530406, 5303892, 5303898, C07K 100, C07K 300, G01N 3353, C12N 900
Patent
active
051069504
ABSTRACT:
A polypeptide-labeled analyte analog for use in an immunoassay is prepared which is capable of binding with a polypeptide partner to provide enzymatic activity such as a ribonuclease or .beta.-galactosidase activity. The polypeptide analog provides a highly sensitive, immunoassay method for determining the amount of an analyte in a sample containing a known analyte in an unknown concentration. To carry out an immunoassay, there is brought together in a medium a sample, the polypeptide-labeled analog of the analyte, an antibody specific for said analyte, a polypeptide partner capable of non-covalently binding with the polypeptide-labeled analyte analog to form a complex having catalytic activity, and a substrate capable of being converted to a reporter molecule by the catalytic activity of said complex. The polypeptide-labeled analyte analog is capable of competitively binding to the antibody and the polypeptide partner, the antibody inhibiting the formation of a catalytically active complex in the absence of analyte, and the concentrations of the antibody, polypeptide partner and polypeptide-labeled analyte are such as to cause varying amounts of analyte to be directly related to the conversion of the substrate to the reporter molecule. Conversion of the substrate to the reporter molecule is then determined, and compared to conversions of substrate to reporter molecule obtained with known concentrations of the analyte.
REFERENCES:
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Farina Peter R.
Golke James R.
Biopharma S.A.
Naff David M.
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