Interaction of duodenase with serpins from human blood serum

N. A. Popykina; I. P. Gladysheva; T. S. Zamolodchikova; N. I. Larionova

doi:10.1023/B:RUBI.0000008895.66892.9a

Interaction of duodenase with serpins from human blood serum

N. A. Popykina, I. P. Gladysheva, T. S. Zamolodchikova, N. I. Larionova

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1 Scopus citations

Abstract

The interaction of duodenase, a new serine protease from a small group of Janus-faced proteases, with serpins, α₁-protease inhibitor (α₁-PI) and antichymotrypsin (ACT) from human blood serum, was studied. The stoichiometry of the inhibition process was found to be 1.2 and 1.3 mol/mol for α₁-PI and ACT, respectively. The presence of a stable enzyme-inhibitory complex duodenase-α₁-PI was confirmed by SDS-PAGE. The formation of the duodenase-ACT complex was not demonstrated; instead, the band of the cleaved inhibitor indicated the ACT hydrolysis. The suicide mechanism of the duodenase interaction with the human blood serpins was proved. The association rate constants (k_a × 10⁵, M^-1 s^-1) were 2.4 ± 0.3 × 10⁵ for α₁-PI and 3.0 ± 0.4 × 10⁵ for ACT. These results indicate the possibility of the regulation of duodenase activity by endogenous serpins.

Original language	English (US)
Pages (from-to)	550-555
Number of pages	6
Journal	Russian Journal of Bioorganic Chemistry
Volume	29
Issue number	6
DOIs	https://doi.org/10.1023/B:RUBI.0000008895.66892.9a
State	Published - Nov 2003
Externally published	Yes

Keywords

Antichymotrypsin
Duodenase
Serpins
α-inhibitor of proteases

ASJC Scopus subject areas

Biochemistry
Organic Chemistry

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10.1023/B:RUBI.0000008895.66892.9a

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title = "Interaction of duodenase with serpins from human blood serum",

abstract = "The interaction of duodenase, a new serine protease from a small group of Janus-faced proteases, with serpins, α1-protease inhibitor (α1-PI) and antichymotrypsin (ACT) from human blood serum, was studied. The stoichiometry of the inhibition process was found to be 1.2 and 1.3 mol/mol for α1-PI and ACT, respectively. The presence of a stable enzyme-inhibitory complex duodenase-α1-PI was confirmed by SDS-PAGE. The formation of the duodenase-ACT complex was not demonstrated; instead, the band of the cleaved inhibitor indicated the ACT hydrolysis. The suicide mechanism of the duodenase interaction with the human blood serpins was proved. The association rate constants (ka × 105, M-1 s-1) were 2.4 ± 0.3 × 105 for α1-PI and 3.0 ± 0.4 × 105 for ACT. These results indicate the possibility of the regulation of duodenase activity by endogenous serpins.",

keywords = "Antichymotrypsin, Duodenase, Serpins, α-inhibitor of proteases",

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

note = "Funding Information: This work was supported by Russian Foundation for Basic Research, project no. 01-04-49848.",

year = "2003",

month = nov,

doi = "10.1023/B:RUBI.0000008895.66892.9a",

language = "English (US)",

volume = "29",

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journal = "Russian Journal of Bioorganic Chemistry",

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TY - JOUR

T1 - Interaction of duodenase with serpins from human blood serum

AU - Popykina, N. A.

AU - Gladysheva, I. P.

AU - Zamolodchikova, T. S.

AU - Larionova, N. I.

N1 - Funding Information: This work was supported by Russian Foundation for Basic Research, project no. 01-04-49848.

PY - 2003/11

Y1 - 2003/11

N2 - The interaction of duodenase, a new serine protease from a small group of Janus-faced proteases, with serpins, α1-protease inhibitor (α1-PI) and antichymotrypsin (ACT) from human blood serum, was studied. The stoichiometry of the inhibition process was found to be 1.2 and 1.3 mol/mol for α1-PI and ACT, respectively. The presence of a stable enzyme-inhibitory complex duodenase-α1-PI was confirmed by SDS-PAGE. The formation of the duodenase-ACT complex was not demonstrated; instead, the band of the cleaved inhibitor indicated the ACT hydrolysis. The suicide mechanism of the duodenase interaction with the human blood serpins was proved. The association rate constants (ka × 105, M-1 s-1) were 2.4 ± 0.3 × 105 for α1-PI and 3.0 ± 0.4 × 105 for ACT. These results indicate the possibility of the regulation of duodenase activity by endogenous serpins.

AB - The interaction of duodenase, a new serine protease from a small group of Janus-faced proteases, with serpins, α1-protease inhibitor (α1-PI) and antichymotrypsin (ACT) from human blood serum, was studied. The stoichiometry of the inhibition process was found to be 1.2 and 1.3 mol/mol for α1-PI and ACT, respectively. The presence of a stable enzyme-inhibitory complex duodenase-α1-PI was confirmed by SDS-PAGE. The formation of the duodenase-ACT complex was not demonstrated; instead, the band of the cleaved inhibitor indicated the ACT hydrolysis. The suicide mechanism of the duodenase interaction with the human blood serpins was proved. The association rate constants (ka × 105, M-1 s-1) were 2.4 ± 0.3 × 105 for α1-PI and 3.0 ± 0.4 × 105 for ACT. These results indicate the possibility of the regulation of duodenase activity by endogenous serpins.

KW - Antichymotrypsin

KW - Duodenase

KW - Serpins

KW - α-inhibitor of proteases

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JO - Russian Journal of Bioorganic Chemistry

JF - Russian Journal of Bioorganic Chemistry

IS - 6

ER -

Interaction of duodenase with serpins from human blood serum

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