@article{ref1,
title="Interaction between duodenase and alpha1-proteinase inhibitor",
journal="Biochemistry (Moscow)",
year="2001",
author="Gladysheva, I. P. and Popykina, N. A. and Zamolodchikova, T. S. and Larionova, N. I.",
volume="66",
number="6",
pages="682-687",
abstract="The interaction between duodenase, a newly recognized serine proteinase belonging to the small group of Janus-faced proteinases, and alpha1-proteinase inhibitor (alpha1-PI) from human serum was investigated. The stoichiometry of the inhibition was 1.2 mol/mol. The presence of a stable enzyme-inhibitor complex was shown by SDS-PAGE. The mechanism of interaction between duodenase and alpha1-PI was shown to be of the suicide type. The equilibrium and inhibition constants are 13 +/- 3 nM and (1.9 +/- 0.3).105 M-1.sec-1, respectively. Based on the association rate constant of the enzyme-inhibitor complex and localization of duodenase and alpha1-PI in identical compartments, alpha1-PI is suggested to be a duodenase inhibitor in vivo.<p /><p>Language: en</p>",
language="en",
issn="0006-2979",
doi="10.1023/a:1010267500296",
url="http://dx.doi.org/10.1023/a:1010267500296"
}