Generation of Catalytically Active Granzyme K fromEscherichia coli Inclusion Bodies and Identification of Efficient Granzyme K Inhibitors in Human Plasma*
- E. Wilharm, M. Parry, D. Jenne
- Biology, ChemistryJournal of Biological Chemistry
- 17 September 1999
Inter-α-trypsin inhibitor and free bikunin have the potential to neutralize extracellular granzyme K activity after T cell degranulation and may thus control unspecific damage of bystander cells at sites of inflammatory reactions.
The Contribution of Residues 192 and 193 to the Specificity of Snake Venom Serine Proteinases*
- S. Braud, M. Parry, R. Maroun, C. Bon, A. Wisner
- Biology, ChemistryJournal of Biological Chemistry
- 21 January 2000
This study demonstrates that Phe193 plays a more significant role than His192 in determining substrate specificity and inhibition resistance in TSV-PA, and possesses a 8–9-fold increased activity for plasminogen and becomes sensitive to bovine pancreatic trypsin inhibitor.
The ternary microplasmin–staphylokinase–microplasmin complex is a proteinase–cofactor–substrate complex in action
- M. Parry, C. Fernández-Catalán, W. Bode
- BiologyNature Structural Biology
- 1 October 1998
This is the first experimental structure of a productive proteinase–cofactor–macromolecular substrate complex and provides a template for the design of improved plasminogen activators and plasmine inhibitors with considerable therapeutical potential.
Kinetic mechanism for the interaction of Hirulog with thrombin.
- M. Parry, J. Maraganore, S. Stone
- Biology, ChemistryBiochemistry
- 13 December 1994
The data were consistent with a mechanism in which the C-terminal region of Hirulog binds to the anion-binding exosite with a dissociation constant of 0.75 microM in the first step, followed by two intramolecular steps with rate constants of about 300 and 30 s-1.
Purification and Characterization of a Milk Clotting Protease fromMucor bacilliformis
- L. Areces, M. B. D. J. Bonino, M. Parry, E. R. Fraile, Héctor M. Fernández, O. Cascone
- Chemistry, MedicineApplied Biochemistry and Biotechnology
- 1 December 1992
An acid protease having milk clotting activity has been isolated from mucor bacilliformis cultures and its instability against heat treatment and its clotting/proteolytic activity ratio indicate that it may be considered as a potential substitute for bovine chymosin.
Cleavage of the thrombin receptor: identification of potential activators and inactivators.
- M. Parry, T. Myles, J. Tschopp, S. Stone
- BiologyBiochemical Journal
- 15 November 1996
In addition to the above cleavage sites, a secondary site for thrombin and other arginine-specific proteases was identified at Arg46, but the cleavage at this site only occurred at very low rates and is unlikely to be significant in vivo.
Molecular basis for the inhibition of thrombin by hirudin.
- S. Stone, A. Betz, M. Parry, M. Jackman, J. Hofsteenge
- Biology, ChemistryAdvances in Experimental Medicine and Biology
- 1993
The amino acid sequence of the 65 residue major form of hirudin, originally isolated from the salivary glands of the European medicinal leech Hirudo medicinalis, is shown and one of the charged residues found in this region of the natural hirUDin is a sulphated tyrosine residue at position 63.
Intrinsic fluorescence changes and rapid kinetics of the reaction of thrombin with hirudin.
- M. Jackman, M. Parry, J. Hofsteenge, S. Stone
- Biology, ChemistryJournal of Biological Chemistry
- 5 August 1992
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