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- W2103871104 abstract "Preparative purification of macromolecules, e.g., proteins, has reached a high standard because of efficient separation materials that are available for this task. However, this is limited to samples containing substantial amounts of the desired protein. When proteins that are present only in minute amounts (e.g., in the μg/L range) must be isolated from a limited supply of complex biological material (e.g., human serum), a one-step method is recommended to obtain the protein in sufficient yield. When suitable antibodies are available, immunopurification often is the method of choice (1), but nonspecific binding of proteins to affinity matrices is a substantial problem because elution with acid or chaotropic agents very often washes off the impurities as well as the analyte (2). Thus, there is a need for methods that allow the specific elution of the desired proteins without eluting the impurities. Specific elution by competing with a low-molecular weight analog is appealing, but suitable analogs may not be available.We wanted to isolate prostate-specific antigen (PSA) from serum and analyze its structure by mass spectrometry. The concentration of PSA in serum from patients with prostate cancer (PCa) ranges from ∼3 to >3000 μg/L, ∼105–107 times less than that of other serum proteins, e.g., albumin. We have developed a general indirect immunosorption method that follows to a certain extent an immunoassay principle developed by Hashida et al. (3) and Ishikawa et al. (4) and makes use of a digoxigenylated anti-analyte antibody. Initially, the …" @default.
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- W2103871104 date "2000-09-01" @default.
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- W2103871104 title "Purification of Prostate-specific Antigen from Serum by Indirect Immunosorption and Elution with a Hapten" @default.
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- W2103871104 doi "https://doi.org/10.1093/clinchem/46.9.1490" @default.
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