A study of aspartyl proteases using intramolecularly quenched fluorogenic peptide substrates

被引：0

作者：

Filippova, IY ^{[1
]}

Lysogorskaya, EN ^{[1
]}

Lavrenova, GI ^{[1
]}

Oksenoit, ES ^{[1
]}

Suvorov, LI ^{[1
]}

Starovoitova, VV ^{[1
]}

机构：

[1] Moscow MV Lomonosov State Univ, Fac Chem, Moscow 119899, Russia

来源：

BIOORGANICHESKAYA KHIMIYA | 2000年 / 26卷 / 03期

关键词：

aspartyl proteases; fluorogenic peptide substrates;

D O I：

暂无

中图分类号：

学科分类号：

摘要：

A series of fluorogenic tetra-, penta-, and hexapeptide substrates of the general structure Abz-X-Phe-Phe-Y-Ded (or -pNa in place of -Ded), where X = Ala, Ala-Ala, or Val-Ala and Y = -, Ala, or Ala-Ala, were proposed, Kinetic parameters of hydrolysis of these substrates by pepsin, cathepsin D, human gastricsin, pig pepsin, calf chymosin, and aspergillopepsin A were determined. The compounds synthesized proved to be effective substrates for aspartyl proteases of diverse origins.

引用

页码：192 / 196

页数：5

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