Glycine-Rich Analogues of Cucurbita maxima Trypsin Inhibitor (CMTI-III) Substituted by Valine in Position 27 Display Relatively Low Antitrypsin Activity

Glycine-Rich Analogues of Cucurbita maxima Trypsin Inhibitor (CMTI-III) Substituted by Valine in... Biol. Chem. Hoppe-Seyler Vol. 374, pp. 851-854, September 1993 Jan ROZYCKI*, Gotfryd KUPRYSZEWSKI*, Krzysztof ROLKA*, Ulf RAGNARSSONÖ, Tomasz ZBYTRYTC, Izabela KROKOSZYNSKAC and Jacek OTLEWSKIC a b Faculty of Chemistry, University of Gdansk, Gdansk, Poland Department of Biochemistry, Biomedical Center, University of Uppsala, Uppsala, Sweden c Institute of Biochemistry, University of Wroclaw, Wroclaw, Poland (Received 4 June 1993) Summary: Five new analogues of the trypsin inhibitor CMTI-III were synthesized by the solid-phase method. All analogues containing a valine residue in position 27 and glycine residues in some or all of the positions 9,11, 14, 17,19, 29 as well as in two cases a norleucine residue in position 8 displayed association equilibrium constants by 6-7 orders of magnitude lower than the native CMTI-III inhibitor. Key terms: Trypsin inhibitor, solid-phase peptide synthesis. In the seeds of plants from the Cucurbitaceae family, a number of polypeptide serine proteinase inhibitors occur, consisting of 28-32 amino acid residues, six of which are cysteines forming 3 disulfide bridges111. The first inhibitors belonging to this group, CMTI-I and CMTI-III (Cucurbita maxima trypsin inhibitor), were isolated in 198012] from squash seeds. The amino acid sequences of these were published in 1983[3J and the three-dimensional structure of CMTI-I http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Biological Chemistry Hoppe-Seyler de Gruyter

Glycine-Rich Analogues of Cucurbita maxima Trypsin Inhibitor (CMTI-III) Substituted by Valine in Position 27 Display Relatively Low Antitrypsin Activity

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Publisher
de Gruyter
Copyright
Copyright © 1993 by the
ISSN
0177-3593
eISSN
1437-4315
DOI
10.1515/bchm3.1993.374.7-12.851
Publisher site
See Article on Publisher Site

Abstract

Biol. Chem. Hoppe-Seyler Vol. 374, pp. 851-854, September 1993 Jan ROZYCKI*, Gotfryd KUPRYSZEWSKI*, Krzysztof ROLKA*, Ulf RAGNARSSONÖ, Tomasz ZBYTRYTC, Izabela KROKOSZYNSKAC and Jacek OTLEWSKIC a b Faculty of Chemistry, University of Gdansk, Gdansk, Poland Department of Biochemistry, Biomedical Center, University of Uppsala, Uppsala, Sweden c Institute of Biochemistry, University of Wroclaw, Wroclaw, Poland (Received 4 June 1993) Summary: Five new analogues of the trypsin inhibitor CMTI-III were synthesized by the solid-phase method. All analogues containing a valine residue in position 27 and glycine residues in some or all of the positions 9,11, 14, 17,19, 29 as well as in two cases a norleucine residue in position 8 displayed association equilibrium constants by 6-7 orders of magnitude lower than the native CMTI-III inhibitor. Key terms: Trypsin inhibitor, solid-phase peptide synthesis. In the seeds of plants from the Cucurbitaceae family, a number of polypeptide serine proteinase inhibitors occur, consisting of 28-32 amino acid residues, six of which are cysteines forming 3 disulfide bridges111. The first inhibitors belonging to this group, CMTI-I and CMTI-III (Cucurbita maxima trypsin inhibitor), were isolated in 198012] from squash seeds. The amino acid sequences of these were published in 1983[3J and the three-dimensional structure of CMTI-I

Journal

Biological Chemistry Hoppe-Seylerde Gruyter

Published: Jan 1, 1993

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