Ingibirovanie ékzogennykh serinovykh proteinaz ingibitorom tripsina iz semian grechikhi IT-1.

I. P. Gladysheva; I. E. Dunaevskii; M. A. Belozerskii; D. P. Gladyshev; A. I. Papisova; N. I. Larionova

Ingibirovanie ékzogennykh serinovykh proteinaz ingibitorom tripsina iz semian grechikhi IT-1.

Translated title of the contribution: Inhibition of exogenous serine proteinases by a trypsin inhibitor from the buckwheat IT-1 seeds

I. P. Gladysheva, I. E. Dunaevskii, M. A. Belozerskii, D. P. Gladyshev, A. I. Papisova, N. I. Larionova

Research output: Contribution to journal › Article › peer-review

2 Scopus citations

Abstract

The possibility of inhibition of exogenous trypsin- and chymotrypsin-like proteinases by a proteinase inhibitor from buckwheat (IT-1) seeds has been studied. The inhibition constants for bovine trypsin and alpha-chymotrypsin and human granulocyte cathepsin G by IT-1 are equal to 1.1, 67 and 200 nm, respectively. The specificity of IT-1 with regard to its primary sequence adjacent to the active center and to its homology with inhibitors pertaining to the potato inhibitor I family has been carried out. It is concluded that by virtue of the basic nature of the P1 (Arg) residue in the active center IT-1 is not capable to bind human granulocyte elastase.

Translated title of the contribution	Inhibition of exogenous serine proteinases by a trypsin inhibitor from the buckwheat IT-1 seeds
Original language	Russian
Pages (from-to)	1530-1535
Number of pages	6
Journal	Biokhimiia (Moscow, Russia)
Volume	60
Issue number	9
State	Published - Sep 1995
Externally published	Yes

ASJC Scopus subject areas

General Chemistry

Cite this

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title = "Ingibirovanie {\'e}kzogennykh serinovykh proteinaz ingibitorom tripsina iz semian grechikhi IT-1.",

abstract = "The possibility of inhibition of exogenous trypsin- and chymotrypsin-like proteinases by a proteinase inhibitor from buckwheat (IT-1) seeds has been studied. The inhibition constants for bovine trypsin and alpha-chymotrypsin and human granulocyte cathepsin G by IT-1 are equal to 1.1, 67 and 200 nm, respectively. The specificity of IT-1 with regard to its primary sequence adjacent to the active center and to its homology with inhibitors pertaining to the potato inhibitor I family has been carried out. It is concluded that by virtue of the basic nature of the P1 (Arg) residue in the active center IT-1 is not capable to bind human granulocyte elastase.",

author = "Gladysheva, \{I. P.\} and Dunaevskii, \{I. E.\} and Belozerskii, \{M. A.\} and Gladyshev, \{D. P.\} and Papisova, \{A. I.\} and Larionova, \{N. I.\}",

year = "1995",

month = sep,

language = "Russian",

volume = "60",

pages = "1530--1535",

journal = "Biokhimiia (Moscow, Russia)",

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number = "9",

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TY - JOUR

T1 - Ingibirovanie ékzogennykh serinovykh proteinaz ingibitorom tripsina iz semian grechikhi IT-1.

AU - Gladysheva, I. P.

AU - Dunaevskii, I. E.

AU - Belozerskii, M. A.

AU - Gladyshev, D. P.

AU - Papisova, A. I.

AU - Larionova, N. I.

PY - 1995/9

Y1 - 1995/9

N2 - The possibility of inhibition of exogenous trypsin- and chymotrypsin-like proteinases by a proteinase inhibitor from buckwheat (IT-1) seeds has been studied. The inhibition constants for bovine trypsin and alpha-chymotrypsin and human granulocyte cathepsin G by IT-1 are equal to 1.1, 67 and 200 nm, respectively. The specificity of IT-1 with regard to its primary sequence adjacent to the active center and to its homology with inhibitors pertaining to the potato inhibitor I family has been carried out. It is concluded that by virtue of the basic nature of the P1 (Arg) residue in the active center IT-1 is not capable to bind human granulocyte elastase.

AB - The possibility of inhibition of exogenous trypsin- and chymotrypsin-like proteinases by a proteinase inhibitor from buckwheat (IT-1) seeds has been studied. The inhibition constants for bovine trypsin and alpha-chymotrypsin and human granulocyte cathepsin G by IT-1 are equal to 1.1, 67 and 200 nm, respectively. The specificity of IT-1 with regard to its primary sequence adjacent to the active center and to its homology with inhibitors pertaining to the potato inhibitor I family has been carried out. It is concluded that by virtue of the basic nature of the P1 (Arg) residue in the active center IT-1 is not capable to bind human granulocyte elastase.

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M3 - Article

C2 - 8562658

AN - SCOPUS:0029362731

SN - 0320-9725

VL - 60

SP - 1530

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JO - Biokhimiia (Moscow, Russia)

JF - Biokhimiia (Moscow, Russia)

IS - 9

ER -

Ingibirovanie ékzogennykh serinovykh proteinaz ingibitorom tripsina iz semian grechikhi IT-1.

Abstract

ASJC Scopus subject areas

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