## Abstract Several new fluorogenic substrates for four proteases were synthesized by coupling the highly fluorescent __7__βaminoβ4βmethylβ2βquinolinone (AMeq) with appropriate amino acids and peptides. Compounds HCl Β· HβAlaβNHβMeq (1) and HCl Β· HβLeuβNHβMeq (2) are substrates for aminopeptidase M,
Sensitive assays for trypsin, elastase, and chymotrypsin using new fluorogenic substrates
β Scribed by M. Zimmerman; B. Ashe; E.C. Yurewicz; G. Patel
- Publisher
- Elsevier Science
- Year
- 1977
- Tongue
- English
- Weight
- 297 KB
- Volume
- 78
- Category
- Article
- ISSN
- 0003-2697
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β¦ Synopsis
Sensitive fluorogenic substrates for trypsin, chymotrypsin, and elastase were prepared. These substrates are amides of an acyl amino acid or peptide with 7-amino-4-methyicoumarin (AMC). The substrates with their respective K,,,/K, ratios given in parentheses are: for chymotrypsin, glutaryl-Phe-AMC (78) and Ala-Ala-Phe-AMC TFA (1660); for trypsin, benzoyl-DL-Arg-AMC (800) and Carbobenzoxy (Cbz)-L-Arg-AMC (5300); for elastase, N-acetyl-Ala-Ala-Pro-Ala-AMC (15,000). The detection limits obtained by using the best substrates and short incubation times are: chymotrypsin, 25 ng; trypsin, 5 ng; and elastase, 2 ng.
π SIMILAR VOLUMES
A new fluorogenic substrate, benzyloxycarbonyl+phenylalanine 4-methylcoumaryl-7-ester, has been developed for determination of the esterase activity of ol-chymotrypsin and related enzymes. Synthesis of the substrate was achieved simply by the carbodiimide condensation of benzyloxycarbonyl+phenylalan