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

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

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 journal › Article › peer-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 contribution	A new fluorogenic substrate of carboxypeptidase H--o-coumaroylphenylalanyl-alanyl-arginine
Original language	Russian
Pages (from-to)	406-412
Number of pages	7
Journal	Bioorganicheskaia khimiia
Volume	20
Issue number	4
State	Published - Apr 1994
Externally published	Yes

ASJC Scopus subject areas

General Medicine

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title = "Novyǐ fluorogennyǐ substrat karboksipeptidazy H--o-kumaroilfenilalanil-alanil-arginin.",

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.",

author = "Pozdnev, {V. F.} and Varlamov, {O. L.} and Grigor'ian, {O. O.} and Gomazkov, {O. A.}",

year = "1994",

month = apr,

language = "Russian",

volume = "20",

pages = "406--412",

journal = "Bioorganicheskaia khimiia",

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T1 - Novyǐ fluorogennyǐ substrat karboksipeptidazy H--o-kumaroilfenilalanil-alanil-arginin.

AU - Pozdnev, V. F.

AU - Varlamov, O. L.

AU - Grigor'ian, O. O.

AU - Gomazkov, O. A.

PY - 1994/4

Y1 - 1994/4

N2 - 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.

AB - 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.

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ER -

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

Abstract

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