Conjugation of the bowman-birk soybean proteinase inhibitor with hydroxyethylstarch

Nathalia I. Larionova; Stepan S. Vartanov; Nadezhda V. Sorokina; Inna P. Gladysheva; Sergey D. Varfolomeyev

doi:10.1007/BF02787993

Conjugation of the bowman-birk soybean proteinase inhibitor with hydroxyethylstarch

Nathalia I. Larionova, Stepan S. Vartanov, Nadezhda V. Sorokina, Inna P. Gladysheva, Sergey D. Varfolomeyev

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

3 Scopus citations

Abstract

The classical Bowman-Birk soybean proteinase inhibitor was modified by hydroxyethylstarch. The modified inhibitor retained the capacity for simultaneous binding of trypsin and human leukocyte elastase. The inhibition constants, K_i, of bovine trypsin, α-chymotrypsin and human leukocyte elastase (HLE) increased not more than 10-, 1.5-, and 20-fold, respectively, on modification of the inhibitor. The less effective inhibition is presumably due to the steric hindrance brought about by the conjugation with polysaccharide molecules. The results obtained indicate the pronounced structure differences of the binding regions for trypsin and chymotrypsin/leukocyte elastase in the modified preparation.

Original language	English (US)
Pages (from-to)	175-182
Number of pages	8
Journal	Applied Biochemistry and Biotechnology - Part A Enzyme Engineering and Biotechnology
Volume	62
Issue number	2-3
DOIs	https://doi.org/10.1007/BF02787993
State	Published - 1997
Externally published	Yes

Keywords

Bowman-Birk soybean inhibitor
Conjugate
Hydroxyethylstarch
Leukocyte elastase
Modification

ASJC Scopus subject areas

Biotechnology
Bioengineering
Biochemistry
Applied Microbiology and Biotechnology
Molecular Biology

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10.1007/BF02787993

Cite this

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title = "Conjugation of the bowman-birk soybean proteinase inhibitor with hydroxyethylstarch",

abstract = "The classical Bowman-Birk soybean proteinase inhibitor was modified by hydroxyethylstarch. The modified inhibitor retained the capacity for simultaneous binding of trypsin and human leukocyte elastase. The inhibition constants, Ki, of bovine trypsin, α-chymotrypsin and human leukocyte elastase (HLE) increased not more than 10-, 1.5-, and 20-fold, respectively, on modification of the inhibitor. The less effective inhibition is presumably due to the steric hindrance brought about by the conjugation with polysaccharide molecules. The results obtained indicate the pronounced structure differences of the binding regions for trypsin and chymotrypsin/leukocyte elastase in the modified preparation.",

keywords = "Bowman-Birk soybean inhibitor, Conjugate, Hydroxyethylstarch, Leukocyte elastase, Modification",

author = "Larionova, {Nathalia I.} and Vartanov, {Stepan S.} and Sorokina, {Nadezhda V.} and Gladysheva, {Inna P.} and Varfolomeyev, {Sergey D.}",

year = "1997",

doi = "10.1007/BF02787993",

language = "English (US)",

volume = "62",

pages = "175--182",

journal = "Applied Biochemistry and Biotechnology - Part A Enzyme Engineering and Biotechnology",

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number = "2-3",

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T1 - Conjugation of the bowman-birk soybean proteinase inhibitor with hydroxyethylstarch

AU - Larionova, Nathalia I.

AU - Vartanov, Stepan S.

AU - Sorokina, Nadezhda V.

AU - Gladysheva, Inna P.

AU - Varfolomeyev, Sergey D.

PY - 1997

Y1 - 1997

N2 - The classical Bowman-Birk soybean proteinase inhibitor was modified by hydroxyethylstarch. The modified inhibitor retained the capacity for simultaneous binding of trypsin and human leukocyte elastase. The inhibition constants, Ki, of bovine trypsin, α-chymotrypsin and human leukocyte elastase (HLE) increased not more than 10-, 1.5-, and 20-fold, respectively, on modification of the inhibitor. The less effective inhibition is presumably due to the steric hindrance brought about by the conjugation with polysaccharide molecules. The results obtained indicate the pronounced structure differences of the binding regions for trypsin and chymotrypsin/leukocyte elastase in the modified preparation.

AB - The classical Bowman-Birk soybean proteinase inhibitor was modified by hydroxyethylstarch. The modified inhibitor retained the capacity for simultaneous binding of trypsin and human leukocyte elastase. The inhibition constants, Ki, of bovine trypsin, α-chymotrypsin and human leukocyte elastase (HLE) increased not more than 10-, 1.5-, and 20-fold, respectively, on modification of the inhibitor. The less effective inhibition is presumably due to the steric hindrance brought about by the conjugation with polysaccharide molecules. The results obtained indicate the pronounced structure differences of the binding regions for trypsin and chymotrypsin/leukocyte elastase in the modified preparation.

KW - Bowman-Birk soybean inhibitor

KW - Conjugate

KW - Hydroxyethylstarch

KW - Leukocyte elastase

KW - Modification

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JO - Applied Biochemistry and Biotechnology - Part A Enzyme Engineering and Biotechnology

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Conjugation of the bowman-birk soybean proteinase inhibitor with hydroxyethylstarch

Abstract

Keywords

ASJC Scopus subject areas

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