Interaction between Duodenase, a Proteinase with Dual Specificity, and Soybean Inhibitors of Bowman-Birk and Kunitz Type

I. P. Gladysheva; T. S. Zamolodchikova; E. A. Sokolova; N. I. Larionova

Interaction between Duodenase, a Proteinase with Dual Specificity, and Soybean Inhibitors of Bowman-Birk and Kunitz Type

I. P. Gladysheva
, T. S. Zamolodchikova
, E. A. Sokolova
, N. I. Larionova

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

Abstract

The interaction between duodenase, which belongs to a group of Janus-faced proteinases, and classical Bowman-Birk (BBI) and Kunitz (STI) type inhibitors from soybean was investigated. Duodenase was shown to interact only with the antichymotrypsin site (Leu-Ser) of BBI, whereas the antitrypsin site (Lys-Ser) of the inhibitor appeared to be vacant and capable of interaction with trypsin. The inhibition constants of duodenase by BBI, the BBI-trypsin complex, and STI were 4,400, and 40 nM, respectively.

Original language	English (US)
Pages (from-to)	1244-1249
Number of pages	6
Journal	Biochemistry (Moscow)
Volume	64
Issue number	11
State	Published - Nov 1999
Externally published	Yes

Keywords

Bowman-birk inhibitor
Duodenase
Inhibition constant
Kunitz inhibitor
Specificity

ASJC Scopus subject areas

Biochemistry

Cite this

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title = "Interaction between Duodenase, a Proteinase with Dual Specificity, and Soybean Inhibitors of Bowman-Birk and Kunitz Type",

abstract = "The interaction between duodenase, which belongs to a group of Janus-faced proteinases, and classical Bowman-Birk (BBI) and Kunitz (STI) type inhibitors from soybean was investigated. Duodenase was shown to interact only with the antichymotrypsin site (Leu-Ser) of BBI, whereas the antitrypsin site (Lys-Ser) of the inhibitor appeared to be vacant and capable of interaction with trypsin. The inhibition constants of duodenase by BBI, the BBI-trypsin complex, and STI were 4,400, and 40 nM, respectively.",

keywords = "Bowman-birk inhibitor, Duodenase, Inhibition constant, Kunitz inhibitor, Specificity",

author = "Gladysheva, \{I. P.\} and Zamolodchikova, \{T. S.\} and Sokolova, \{E. A.\} and Larionova, \{N. I.\}",

year = "1999",

month = nov,

language = "English (US)",

volume = "64",

pages = "1244--1249",

journal = "Biochemistry (Moscow)",

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T1 - Interaction between Duodenase, a Proteinase with Dual Specificity, and Soybean Inhibitors of Bowman-Birk and Kunitz Type

AU - Gladysheva, I. P.

AU - Zamolodchikova, T. S.

AU - Sokolova, E. A.

AU - Larionova, N. I.

PY - 1999/11

Y1 - 1999/11

N2 - The interaction between duodenase, which belongs to a group of Janus-faced proteinases, and classical Bowman-Birk (BBI) and Kunitz (STI) type inhibitors from soybean was investigated. Duodenase was shown to interact only with the antichymotrypsin site (Leu-Ser) of BBI, whereas the antitrypsin site (Lys-Ser) of the inhibitor appeared to be vacant and capable of interaction with trypsin. The inhibition constants of duodenase by BBI, the BBI-trypsin complex, and STI were 4,400, and 40 nM, respectively.

AB - The interaction between duodenase, which belongs to a group of Janus-faced proteinases, and classical Bowman-Birk (BBI) and Kunitz (STI) type inhibitors from soybean was investigated. Duodenase was shown to interact only with the antichymotrypsin site (Leu-Ser) of BBI, whereas the antitrypsin site (Lys-Ser) of the inhibitor appeared to be vacant and capable of interaction with trypsin. The inhibition constants of duodenase by BBI, the BBI-trypsin complex, and STI were 4,400, and 40 nM, respectively.

KW - Bowman-birk inhibitor

KW - Duodenase

KW - Inhibition constant

KW - Kunitz inhibitor

KW - Specificity

UR - https://www.scopus.com/pages/publications/0033217716

UR - https://www.scopus.com/pages/publications/0033217716#tab=citedBy

M3 - Article

C2 - 10611528

AN - SCOPUS:0033217716

SN - 0006-2979

VL - 64

SP - 1244

EP - 1249

JO - Biochemistry (Moscow)

JF - Biochemistry (Moscow)

IS - 11

ER -

Interaction between Duodenase, a Proteinase with Dual Specificity, and Soybean Inhibitors of Bowman-Birk and Kunitz Type

Abstract

Keywords

ASJC Scopus subject areas

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