✦ LIBER ✦

Intramolecularly quenched fluorogenic substrates for hydrolytic enzymes

✍ Scribed by A. Yaron; A. Carmel; E. Katchalski-Katzir

Publisher: Elsevier Science
Year: 1979
Tongue: English
Weight: 706 KB
Volume: 95
Category: Article
ISSN: 0003-2697
DOI: 10.1016/0003-2697(79)90210-0

No coin nor oath required. For personal study only.

✦ Synopsis

The design and application of a recently developed type of fluorogenic substrates for proteolytic enzymes is reviewed. The substrates consist of peptide chains constructed to match the specificity of the particular enzyme and to bear a suitable chromophore at each side of the cleavable bond. One of the chromophores is a fluorescent group and the other is a quencher that causes a great reduction of fluorescence intensity of the fluorophore, either by direct intramolecular encounter or by radiationless resonance energy transfer. Enzymic cleavage of the molecule is followed by release of fluorescence as the result of cancelling the quenching interaction between the chromophores. The properties of such substrates and their possible future applications are discussed.

📜 SIMILAR VOLUMES

Intramolecularly quenched fluorogenic pe

Intramolecularly quenched fluorogenic peptide substrates for human renin

✍ Maria C.F. Oliveira; Izaura Y. Hirata; Jair R. Chagas; Paulo Boschcov; Roseli A. 📂 Article 📅 1992 🏛 Elsevier Science 🌐 English ⚖ 591 KB

Six intramolecularly quenched fluorogenic peptides related to the sequences Phe8 to His13, His6 to His13, and Tyr4 to His13 of the human angiotensinogen, containing o-aminobenzoyl (Abz) and ethylenediamine dinitrophenyl (EDDnp) groups at amino- and carboxyl-terminal amino acids residues, were synthe

Intramolecularly quenched fluorogenic te

Intramolecularly quenched fluorogenic tetrapeptide substrates for tissue and plasma kallikreins

✍ Jair R. Chagas; Luiz Juliano; Eline S. Prado 📂 Article 📅 1991 🏛 Elsevier Science 🌐 English ⚖ 786 KB

Five intramolecularly quenched fluorogenic substrates for arginyl hydrolases with the sequence Abz-Phe-Arg-X-Y-EDDnp (X = Arg or Ser; Y = Val, Pro, or Arg) were synthesized by classical solution methods. Kinetics of their hydrolysis by tissue and plasma kallikreins, trypsin, and thrombin characteriz

Internally Quenched Fluorogenic Substrat

Internally Quenched Fluorogenic Substrate for Furin

✍ H. Angliker; U. Neumann; S.S. Molloy; G. Thomas 📂 Article 📅 1995 🏛 Elsevier Science 🌐 English ⚖ 300 KB

A new substrate for furin, Abz-Arg-Val-Lys-ArgGly-Leu-Ala-Tyr \(\left(\mathrm{NO}_{2}\right)\)-Asp-OH, has been synthesized and characterized. The peptide is an internally quenched fluorogenic substrate. The kinetic parameters are \(K_{m}=3.8 \mu \mathrm{M}, k_{\text {cat }}=29.3 \mathrm{~s}^{-1}\),

A Versatile Periodate-Coupled Fluorogeni

A Versatile Periodate-Coupled Fluorogenic Assay for Hydrolytic Enzymes

✍ Fabrizio Badalassi; Denis Wahler; Gérard Klein; Paolo Crotti; Jean-Louis Reymond 📂 Article 📅 2000 🏛 John Wiley and Sons 🌐 English ⚖ 107 KB

A Versatile Periodate-Coupled Fluorogeni

A Versatile Periodate-Coupled Fluorogenic Assay for Hydrolytic Enzymes

✍ Fabrizio Badalassi; Denis Wahler; Gérard Klein; Paolo Crotti; Jean-Louis Reymond 📂 Article 📅 2000 🏛 John Wiley and Sons 🌐 English ⚖ 106 KB

A fluorogenic substrate for angiotensin-

A fluorogenic substrate for angiotensin-converting enzyme

✍ Anders Persson; Irwin B. Wilson 📂 Article 📅 1977 🏛 Elsevier Science 🌐 English ⚖ 406 KB

A fluorogenic substrate for the angiotensin-converting enzyme (EC 3.4.15.1) is presented: para-nitrobenzyloxycarbonylglycyl-~-tryptophylglycine. The assay is based upon relief of the internal quenching of tryptophan fluorescence by the nitrobenzyl group when the substrate is enzymatically hydrolyze