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

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

Research output: Contribution to journalArticle

1 Citation (Scopus)

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.

Original languageEnglish (US)
Pages (from-to)1104-1107
Number of pages4
JournalBiochemistry (Moscow)
Volume64
Issue number10
StatePublished - Oct 1 1999

Fingerprint

Fagopyrum
Trypsin Inhibitors
Trypsin
Seed
Rate constants
Seeds
Kinetics
Enzyme Inhibitors
Association reactions

All Science Journal Classification (ASJC) codes

  • Biochemistry

Cite this

Gladysheva, I., Gladyshev, D. P., Dunaevsky, Y. E., Belozersky, M. A., & Larionova, N. I. (1999). Kinetics of Interaction of Trypsin with an Anionic Inhibitor of Trypsin BWI-1a from Buckwheat Seeds. Biochemistry (Moscow), 64(10), 1104-1107.

Kinetics of Interaction of Trypsin with an Anionic Inhibitor of Trypsin BWI-1a from Buckwheat Seeds. / Gladysheva, Inna; Gladyshev, D. P.; Dunaevsky, Y. E.; Belozersky, M. A.; Larionova, N. I.

In: Biochemistry (Moscow), Vol. 64, No. 10, 01.10.1999, p. 1104-1107.

Research output: Contribution to journalArticle

Gladysheva, I, Gladyshev, DP, Dunaevsky, YE, Belozersky, MA & Larionova, NI 1999, 'Kinetics of Interaction of Trypsin with an Anionic Inhibitor of Trypsin BWI-1a from Buckwheat Seeds', Biochemistry (Moscow), vol. 64, no. 10, pp. 1104-1107.
Gladysheva I, Gladyshev DP, Dunaevsky YE, Belozersky MA, Larionova NI. Kinetics of Interaction of Trypsin with an Anionic Inhibitor of Trypsin BWI-1a from Buckwheat Seeds. Biochemistry (Moscow). 1999 Oct 1;64(10):1104-1107.
Gladysheva, Inna ; Gladyshev, D. P. ; Dunaevsky, Y. E. ; Belozersky, M. A. ; Larionova, N. I. / Kinetics of Interaction of Trypsin with an Anionic Inhibitor of Trypsin BWI-1a from Buckwheat Seeds. In: Biochemistry (Moscow). 1999 ; Vol. 64, No. 10. pp. 1104-1107.
@article{e281d67e90ff40f9874893dfa0093fcf,
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.",
author = "Inna Gladysheva and Gladyshev, {D. P.} and Dunaevsky, {Y. E.} and Belozersky, {M. A.} and Larionova, {N. I.}",
year = "1999",
month = "10",
day = "1",
language = "English (US)",
volume = "64",
pages = "1104--1107",
journal = "Biochemistry (Moscow)",
issn = "0006-2979",
publisher = "Maik Nauka-Interperiodica Publishing",
number = "10",

}

TY - JOUR

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

AU - Gladysheva, Inna

AU - Gladyshev, D. P.

AU - Dunaevsky, Y. E.

AU - Belozersky, M. A.

AU - Larionova, N. I.

PY - 1999/10/1

Y1 - 1999/10/1

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.

UR - http://www.scopus.com/inward/record.url?scp=0033202946&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0033202946&partnerID=8YFLogxK

M3 - Article

VL - 64

SP - 1104

EP - 1107

JO - Biochemistry (Moscow)

JF - Biochemistry (Moscow)

SN - 0006-2979

IS - 10

ER -