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Protease composition of exocytosed human skin mast cell protease-proteoglycan complexes: Tryptase resides in a complex distinct from chymase and carboxypeptidase
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Regulation of tryptase from human lung mast cells by heparin. Stabilization of the active tetramer
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Human β-tryptase is a ring-like tetramer with active sites facing a central pore
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A novel heparin-dependent processing pathway for human tryptase: Autocatalysis followed by activation with dipeptidyl peptidase I
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Sakai, K., Ren, S., and Schwartz, L. B. (1996) A novel heparin-dependent processing pathway for human tryptase: autocatalysis followed by activation with dipeptidyl peptidase I, J. Clin. Invest. 97, 988-995.
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Human skin tryptase: Kinetic characterization of its spontaneous inactivation
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Inactivation of human lung tryptase: Evidence for a re-activatable tetrameric intermediate and active monomers
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Regulation of human mast cell β-tryptase: Conversion of inactive monomer to active tetramer at acid pH
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Ren, S. L., Sakai, K., and Schwartz, L. B. (1998) Regulation of human mast cell β-tryptase: Conversion of inactive monomer to active tetramer at acid pH, J. Immunol. 160, 4561-4569.
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Human tryptase fibrinogenolysis is optimal at acidic pH and generates anticoagulant fragments in the presence of the anti-tryptase monoclonal antibody B12
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Ren, S., Lawson, A. E., Carr, M., Baumgarten, C. M., and Schwartz, L. B. (1997) Human tryptase fibrinogenolysis is optimal at acidic pH and generates anticoagulant fragments in the presence of the anti-tryptase monoclonal antibody B12, J. Immunol. 159, 3540-3548.
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Structural requirements and mechanism for heparin-induced activation of a recombinant mouse mast cell tryptase, mouse mast cell protease-6: Formation of active tryptase monomers in the presence of low molecular weight heparin
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Hallgren, J., Spillmann, D., and Pejler, G. (2001) Structural requirements and mechanism for heparin-induced activation of a recombinant mouse mast cell tryptase, mouse mast cell protease-6: formation of active tryptase monomers in the presence of low molecular weight heparin, J. Biol. Chem. 276, 42774-42781.
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Immunologic and physicochemical evidence for conformational changes occurring on conversion of human mast cell tryptase from active tetramer to inactive monomer: Production of monoclonal antibodies recognizing active tryptase
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0030087557
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Expression and purification of recombinant human tryptase in a baculovirus system
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Sakai, K., Long, S. D., Pettit, D. A. D., Cabral, G. A., and Schwartz, L. B. (1996) Expression and purification of recombinant human tryptase in a baculovirus system, Protein Expression Purif. 7, 67-73.
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Development of a new, more sensitive immunoassay for human tryptase: Use in systemic anaphylaxis
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Schwartz, L. B., Bradford, T. R., Rouse, C., Irani, A.-M., Rasp, G., Van der Zwan, J. K., and Van Der Linden, P.-W. G. (1994) Development of a new, more sensitive immunoassay for human tryptase: Use in systemic anaphylaxis, J. Clin. Immunol. 14, 190-204.
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Regulation of human mast cell tryptase. Effects of enzyme concentration, ionic strength and the structure and negative charge density of polysaccharides
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The active site of antithrombin. Release of the same proteolytically cleaved form of the inhibitor from complexes with factor IXa, factor Xa, and thrombin
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Studies on human plasma alpha 2-macroglobulin-enzyme interactions. Evidence for proteolytic modification of the subunit chain structure
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