Novyǐ fluorogennyǐ substrat karboksipeptidazy H--o-kumaroilfenilalanil-alanil-arginin.

Translated title of the contribution: A new fluorogenic substrate of carboxypeptidase H--o-coumaroylphenylalanyl-alanyl-arginine

V. F. Pozdnev, O. L. Varlamov, O. O. Grigor'ian, O. A. Gomazkov

    Research output: Contribution to journalArticlepeer-review

    1 Scopus citations

    Abstract

    New fluorogenic substrate of carboxypeptidase H, Cum-Phe-Ala-Arg-OH, is hydrolyzed by this enzyme to give Cum-Phe-Ala-OH, which is completely extracted by chloroform from the reaction mixture and whose fluorescence increases remarkably by the presence of triethylamine. When the hydrolysis of the novel substrate is compared with Dns-Phe-Ala-Arg-OH, the former has Km twice as low (30 microM) and kcat four times as high (5.8 s-1). Activation of the enzyme by Co2+ in reactions with the two substrates was also studied. The novel substrate is useful for the enzyme's assay in homogenates of various animal tissues.

    Translated title of the contributionA new fluorogenic substrate of carboxypeptidase H--o-coumaroylphenylalanyl-alanyl-arginine
    Original languageRussian
    Pages (from-to)406-412
    Number of pages7
    JournalBioorganicheskaia khimiia
    Volume20
    Issue number4
    StatePublished - Apr 1 1994

    ASJC Scopus subject areas

    • Medicine(all)

    Fingerprint Dive into the research topics of 'A new fluorogenic substrate of carboxypeptidase H--o-coumaroylphenylalanyl-alanyl-arginine'. Together they form a unique fingerprint.

    Cite this