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High-affinity binding of two molecules of cysteine proteinases to low-molecular-weight kininogen

1995; Wiley; Volume: 4; Issue: 9 Linguagem: Inglês

10.1002/pro.5560040922

1469-896X

Boris Turk, Veronika Stoka, Ingemar Björk, Christian Boudier, Gunnar Johansson, Iztok Dolenc, Adrijana C̆olić, Joseph G. Bieth, Vito Türk,

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Protein ScienceVolume 4, Issue 9 p. 1874-1880 ArticleFree Access High-affinity binding of two molecules of cysteine proteinases to low-molecular-weight kininogen Boris Turk, Corresponding Author Boris Turk boris.turk@vmk.slu.se Department of Veterinary Medical Chemistry, Swedish University of Agricultural Sciences, The Biomedical Center, Uppsala, Sweden Department of Biochemistry & Molecular Biology, J. Stefan Institute, Jamova 39, Ljubljana, SloveniaDepartment of Veterinary Medical Chemistry, The Biomedical Center, POB 575, S-751 23 Uppsala, SwedenSearch for more papers by this authorVeronika Stoka, Veronika Stoka Department of Biochemistry & Molecular Biology, J. Stefan Institute, Jamova 39, Ljubljana, SloveniaSearch for more papers by this authorIngemar Björk, Ingemar Björk Department of Veterinary Medical Chemistry, Swedish University of Agricultural Sciences, The Biomedical Center, Uppsala, SwedenSearch for more papers by this authorChristian Boudier, Christian Boudier INSERM U392, Universite Louis Pasteur de Strasbourg, Illkirch, FranceSearch for more papers by this authorGunnar Johansson, Gunnar Johansson Department of Biochemistry, Uppsala University, The Biomedical Center, Uppsala, SwedenSearch for more papers by this authorIztok Dolenc, Iztok Dolenc Department of Biochemistry & Molecular Biology, J. Stefan Institute, Jamova 39, Ljubljana, SloveniaSearch for more papers by this authorAdrijana Colic, Adrijana Colic Department of Biochemistry & Molecular Biology, J. Stefan Institute, Jamova 39, Ljubljana, SloveniaSearch for more papers by this authorJoseph G. Bieth, Joseph G. Bieth INSERM U392, Universite Louis Pasteur de Strasbourg, Illkirch, FranceSearch for more papers by this authorVito Turk, Vito Turk Department of Biochemistry & Molecular Biology, J. Stefan Institute, Jamova 39, Ljubljana, SloveniaSearch for more papers by this author Boris Turk, Corresponding Author Boris Turk boris.turk@vmk.slu.se Department of Veterinary Medical Chemistry, Swedish University of Agricultural Sciences, The Biomedical Center, Uppsala, Sweden Department of Biochemistry & Molecular Biology, J. Stefan Institute, Jamova 39, Ljubljana, SloveniaDepartment of Veterinary Medical Chemistry, The Biomedical Center, POB 575, S-751 23 Uppsala, SwedenSearch for more papers by this authorVeronika Stoka, Veronika Stoka Department of Biochemistry & Molecular Biology, J. Stefan Institute, Jamova 39, Ljubljana, SloveniaSearch for more papers by this authorIngemar Björk, Ingemar Björk Department of Veterinary Medical Chemistry, Swedish University of Agricultural Sciences, The Biomedical Center, Uppsala, SwedenSearch for more papers by this authorChristian Boudier, Christian Boudier INSERM U392, Universite Louis Pasteur de Strasbourg, Illkirch, FranceSearch for more papers by this authorGunnar Johansson, Gunnar Johansson Department of Biochemistry, Uppsala University, The Biomedical Center, Uppsala, SwedenSearch for more papers by this authorIztok Dolenc, Iztok Dolenc Department of Biochemistry & Molecular Biology, J. Stefan Institute, Jamova 39, Ljubljana, SloveniaSearch for more papers by this authorAdrijana Colic, Adrijana Colic Department of Biochemistry & Molecular Biology, J. Stefan Institute, Jamova 39, Ljubljana, SloveniaSearch for more papers by this authorJoseph G. Bieth, Joseph G. Bieth INSERM U392, Universite Louis Pasteur de Strasbourg, Illkirch, FranceSearch for more papers by this authorVito Turk, Vito Turk Department of Biochemistry & Molecular Biology, J. Stefan Institute, Jamova 39, Ljubljana, SloveniaSearch for more papers by this author First published: September 1995 https://doi.org/10.1002/pro.5560040922Citations: 23AboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL Share a linkShare onFacebookTwitterLinkedInRedditWechat Abstract Human low-molecular-weight kininogen (LK) was shown by fluorescence titration to bind two molecules of ca-thepsins L and S and papain with high affinity. By contrast, binding of a second molecule of cathepsin H was much weaker. The 2:1 binding stoichiometry was confirmed by titration monitored by loss of enzyme activity and by sedimentation velocity experiments. The kinetics of binding of cathepsins L and S and papain showed the two proteinase binding sites to have association rate constants kass, I = 10.7-24.5 × 106 M−1 s−1 and kass, 2 = 0.83-1.4 × 106 M−1 s−1. Comparison of these kinetic constants with previous data for intact LK and its separated domains indicate that the faster-binding site is also the tighter-binding site and is present on domain 3, whereas the slower-binding, lower-affinity site is on domain 2. 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