Kinetics of Interaction of Trypsin with an Anionic Inhibitor of Trypsin BWI-1a from Buckwheat Seeds

I. P. Gladysheva; D. P. Gladyshev; Y. E. Dunaevsky; M. A. Belozersky; N. I. Larionova

Kinetics of Interaction of Trypsin with an Anionic Inhibitor of Trypsin BWI-1a from Buckwheat Seeds

I. P. Gladysheva, D. P. Gladyshev, Y. E. Dunaevsky, M. A. Belozersky, N. I. Larionova

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

Abstract

The kinetics of binding of bovine trypsin to a proteinaceous inhibitor of trypsin from buckwheat seeds (BWI-1a) has been studied. The association rate constant (k_ass) was 2.2-10⁶ M^-1 sec^-1 and the dissociation rate constant (k_off) of the enzyme-inhibitor complex was 3.5·10^-3 sec^-1; the inhibition constant K_i was 1.5 nM. The inhibitor BWI-1a is of the slow, tightly binding type. The mechanism of the inhibition of bovine trypsin by the trypsin inhibitor BWI-1a was studied. The mechanism of inhibition was found to involve two steps according to the kinetic data.

Original language	English (US)
Pages (from-to)	1104-1107
Number of pages	4
Journal	Biochemistry (Moscow)
Volume	64
Issue number	10
State	Published - Oct 1999
Externally published	Yes

Keywords

Buckwheat
Inhibition constant
Kinetics
Mechanism
Proteinase inhibitor

ASJC Scopus subject areas

Biochemistry

Cite this

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title = "Kinetics of Interaction of Trypsin with an Anionic Inhibitor of Trypsin BWI-1a from Buckwheat Seeds",

abstract = "The kinetics of binding of bovine trypsin to a proteinaceous inhibitor of trypsin from buckwheat seeds (BWI-1a) has been studied. The association rate constant (kass) was 2.2-106 M-1 sec-1 and the dissociation rate constant (koff) of the enzyme-inhibitor complex was 3.5·10-3 sec-1; the inhibition constant Ki was 1.5 nM. The inhibitor BWI-1a is of the slow, tightly binding type. The mechanism of the inhibition of bovine trypsin by the trypsin inhibitor BWI-1a was studied. The mechanism of inhibition was found to involve two steps according to the kinetic data.",

keywords = "Buckwheat, Inhibition constant, Kinetics, Mechanism, Proteinase inhibitor",

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T1 - Kinetics of Interaction of Trypsin with an Anionic Inhibitor of Trypsin BWI-1a from Buckwheat Seeds

AU - Gladysheva, I. P.

AU - Gladyshev, D. P.

AU - Dunaevsky, Y. E.

AU - Belozersky, M. A.

AU - Larionova, N. I.

PY - 1999/10

Y1 - 1999/10

N2 - The kinetics of binding of bovine trypsin to a proteinaceous inhibitor of trypsin from buckwheat seeds (BWI-1a) has been studied. The association rate constant (kass) was 2.2-106 M-1 sec-1 and the dissociation rate constant (koff) of the enzyme-inhibitor complex was 3.5·10-3 sec-1; the inhibition constant Ki was 1.5 nM. The inhibitor BWI-1a is of the slow, tightly binding type. The mechanism of the inhibition of bovine trypsin by the trypsin inhibitor BWI-1a was studied. The mechanism of inhibition was found to involve two steps according to the kinetic data.

AB - The kinetics of binding of bovine trypsin to a proteinaceous inhibitor of trypsin from buckwheat seeds (BWI-1a) has been studied. The association rate constant (kass) was 2.2-106 M-1 sec-1 and the dissociation rate constant (koff) of the enzyme-inhibitor complex was 3.5·10-3 sec-1; the inhibition constant Ki was 1.5 nM. The inhibitor BWI-1a is of the slow, tightly binding type. The mechanism of the inhibition of bovine trypsin by the trypsin inhibitor BWI-1a was studied. The mechanism of inhibition was found to involve two steps according to the kinetic data.

KW - Buckwheat

KW - Inhibition constant

KW - Kinetics

KW - Mechanism

KW - Proteinase inhibitor

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AN - SCOPUS:0033202946

SN - 0006-2979

VL - 64

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JO - Biochemistry (Moscow)

JF - Biochemistry (Moscow)

IS - 10

ER -

Kinetics of Interaction of Trypsin with an Anionic Inhibitor of Trypsin BWI-1a from Buckwheat Seeds

Abstract

Keywords

ASJC Scopus subject areas

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