Print Email Facebook Twitter Substrate specificity of tissue-type and urokinase-type plasminogen activators Title Substrate specificity of tissue-type and urokinase-type plasminogen activators Author Rijken, D.C. Groeneveld, E. Gaubius Instituut TNO Publication year 1991 Abstract Recent studies suggest that plasminogen activators not only hydrolyse a specific arginine-valine bond in plasminogen, but may also cleave other proteins such as fibronectin. We studied the substrate specificity, particularly the preference for arginyl over lysyl peptide bonds, of tissue-type plasminogen activator (t-PA) as well as of two-chain urokinase-type plasminogen activator (u-PA). The arginine/lysine preference was determined with three pairs of tripeptidyl-p-nitroanilide substrates having either arginine or lysine in the P1 position and varied from 5.2 to 14.1 for u-PA and from 55.6 to 99.8 for t-PA. It was concluded that both t-PA and u-PA preferred arginyl to lysyl peptide bonds. However, u-PA had a significantly lower arginine/lysine preference than t-PA, indicating that u-PA represents a less specific proteinase. This may point to functions of u-PA other than plasminogen activation, which involve cleavage of lysyl bonds. Subject BiologyAmino Acid SequenceBinding SitesCells, CulturedEnzyme PrecursorsHumanHydrogen-Ion ConcentrationKidneyKineticsMelanomaMolecular Sequence DataPlasminogen ActivatorsSubstrate SpecificitySupport, Non-U.S. Gov'tTissue Plasminogen ActivatorTumor Cells, CulturedUrinary Plasminogen Activator To reference this document use: http://resolver.tudelft.nl/uuid:d573f7e9-08d2-4025-9225-8655e25ab145 TNO identifier 231514 ISSN 0006-291X Source Biochemical and Biophysical Research Communications, 174 (2), 432-438 Document type article Files To receive the publication files, please send an e-mail request to TNO Library.