Synthesis of dinitrophenyltetrapeptides as chromophoric substrates of endoproteinases

Autor:	M. A. Samartsev, S. V. Kulikov, N. Yu. Sokolova, S. V. Rodin
Rok vydání:	1983
Předmět:	chemistry.chemical_classification animal structures integumentary system chemistry Arginine Stereochemistry Enzymatic hydrolysis embryonic structures Plant Science General Chemistry General Biochemistry Genetics and Molecular Biology Amino acid
Zdroj:	Chemistry of Natural Compounds. 19:469-475
ISSN:	1573-8388 0009-3130
DOI:	10.1007/bf00575711
Popis:	The synthesis has been performed of ten tetrapeptides of the general formula Dnp-Gly-Gly-X-Arg-OH, where X = Val, Phe, Abu, Asp (OBut), Asp, Met, D-Phe, Ser, Thr, or Trp. The synthesis was carried out with Dnp-Gly-Gly-ONp, activated esters of protected amino acids, and arginine with an unprotected carboxy group. The coefficients of molar extinction of the tetrapeptides at 660 nm are given. It has been shown that the peptides can be used to determine the activities of neutral and alkaline proteinases from various sources, the peptides with X = Phe, Met, and Abu exhibiting the highest sensitivity to enzymatic hydrolysis.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::d7087ac473e045f28dec5801a840671f https://doi.org/10.1007/bf00575711 Zobrazit plný text záznamu Full text from SpringerLink