LEKTI domain 15 is a functional Kazal-type proteinase inhibitor

Vitzithum, Klaus, Lauber, Thomas, Kreutzmann, Peter, Schulz, Axel, Sommerhoff, Christian P., Rosch, Paul and Marx, Ute C. (2008) LEKTI domain 15 is a functional Kazal-type proteinase inhibitor. Protein Expression and Purification, 57 1: 45-56. doi:10.1016/j.pep.2007.08.012

Author Vitzithum, Klaus
Lauber, Thomas
Kreutzmann, Peter
Schulz, Axel
Sommerhoff, Christian P.
Rosch, Paul
Marx, Ute C.
Title LEKTI domain 15 is a functional Kazal-type proteinase inhibitor
Journal name Protein Expression and Purification   Check publisher's open access policy
ISSN 1046-5928
Publication date 2008-01
Sub-type Article (original research)
DOI 10.1016/j.pep.2007.08.012
Volume 57
Issue 1
Start page 45
End page 56
Total pages 12
Place of publication United States
Publisher Academic Press
Language eng
Formatted abstract
The multidomain proteinase inhibitor LEKTI (lympho-epithelial Kazal-type related inhibitor) consists of 15 potential serine proteinase inhibitory domains. In various diseases such as the severe skin disorder Netherton syndrome as well as atopy, defects in the gene
encoding LEKTI have been identified that generate premature termination codons of translation, suggesting a specific role of the COOH-terminal part of LEKTI in healthy individuals. We overexpressed and purified a sequence comprising the 15th domain of LEKTI for further characterisation. Here, we present a high yield expression system for recombinant production and efficient purification of LEKTI domain 15 as a highly soluble protein with a uniform disulfide pattern that is identical to that of other known Kazal-type inhibitors. Also, the expected P1P10 site was confirmed. LEKTI domain 15 is a well-structured protein as verified by circular dichroism (CD) spectroscopy and a tight-binding and stable inhibitor of the serine proteinase trypsin. These findings confirm the designation of domain 15 as a proteinase inhibitor of the Kazal family.

Keyword Recombinant Production
Serine-protease inhibitor
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status UQ

Document type: Journal Article
Sub-type: Article (original research)
Collection: Institute for Molecular Bioscience - Publications
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Citation counts: TR Web of Science Citation Count  Cited 7 times in Thomson Reuters Web of Science Article | Citations
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Created: Thu, 03 Sep 2009, 10:36:33 EST by Mr Andrew Martlew on behalf of Institute for Molecular Bioscience