T-kinin is released from T-kininogen by consecutive cleavage by cathespin E-like proteinase and 72 kDa proteinase |
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| Institution: | 1. Department of Pathology, Microbiology and Immunology, Vanderbilt University, Nashville, TN, USA;2. Department of Bioengineering and Organic Chemistry, Tomsk Polytechnic University, Tomsk, Russia;3. Dyax Corp., Burlington, MA, USA;4. Department of Molecular Medicine and Surgery, Karolinska Institutet and University Hospital, Stockholm, Sweden;5. Institute of Clinical Chemistry and Laboratory Medicine, University Medical Center Hamburg-Eppendorf, Hamburg, Germany;6. Department of Hematology and Oncology, Cleveland Clinic, Cleveland, OH, USA;7. Joslin Diabetes Center, Harvard Medical School, Boston, MA, USA |
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| Abstract: | Using highly purified T-kininogen and cathepsin E-like proteinase and 72 kDa proteinase in rat spleen, the release of T-kinin from T-kininogen was found to occur by consecutive cleavage by cathespin E-like proteinase and 72 kDa proteinase. 72 kDa proteinase seems to be serine proteinase, because it was completely inhibited by diisopropyl fluorophosphate but not by pepstatin, leupeptin and bestatin. |
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