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- W973038548 abstract "This chapter describes assay methods for arginine/lysine carboxypeptidases. The most frequently employed assay for carboxypeptidase H utilizes a fluorescent substrate, either 5-dimethylaminonaphthalene-l-sulfonyl (dansyl; Dns)-Phe-Leu-Arg or Dns-Phe-Ala-Arg. After the enzymatic reaction, the solution is acidified and extracted with chloroform. The substrate remains in the aqueous phase, and the hydrophobic product is extracted into the chloroform layer. The assays based on fluorescent substrates are more sensitive than those using the UV-absorbing substrates. As the reaction, extraction, and fluorescence measurements can all be done in a single tube, the assay is quite convenient. Similar methods using radiolabeled peptides have also been employed to increase the sensitivity. The use of protected tripeptides as substrates, especially with crude samples, can lead to very high background hydrolysis by enzymes other than arginine/lysine metallocarboxypeptidases. For synthesis of Dns-Ala-Arg, the substrate is easily synthesized by dansylating the dipeptide Ala-Arg and can be purified by thin-layer chromatography (TLC) or high-performance liquid chromatography (HPLC). The synthesis can be carried out with Ala-Arg in amounts ranging from 50 to 1000 mg." @default.
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- W973038548 date "1991-01-01" @default.
- W973038548 modified "2023-10-02" @default.
- W973038548 title "Assays for Arginine/Lysine Carboxypeptidases: Carboxypeptidases H (E; Enkephalin Convertase), M, and N" @default.
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- W973038548 doi "https://doi.org/10.1016/b978-0-12-185261-0.50030-7" @default.
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