Purification and characterization of a novel fibrinolytic enzyme from Whitmania pigra Whitman
Research article published in Protein expression and purification (2020)
Abstract
Developing an effective fibrinolytic drug for treating thrombolysis with minimal undesirable side effects is of great importance. In the current study, an optimum solvent was selected for the extraction of fibrinolytic active components. Furthermore, a strong fibrinolytic enzyme named WPI01 was purified from Whitmania pigra Whitman through various chromatographic steps. WPI01 has a molecular mass of 27044.297 Da, and the N-terminal 8 amino acid sequence was determined as VVGGVEAR. WPI01 was stable within the pH range of 6.0-10.0 and with maximum fibrinolytic activity at 40 °C and a pH of 8.0. At 500 U/mL, WPI01 induced 50.59% blood clot reduction in vitro within 6 h, which was higher than that induced by urokinase at 1000 U/mL. In an analysis of the plasminogen activator activity, WPI01 produced obvious halos on heated and unheated fibrin plates, suggesting that WPI01 may not only act as a plasminogen activator but also degrade fibrin clots directly, and more study is needed to support this. In conclusion, WPI01 is obviously different from known fibrinolytic enzymes in terms of substrate specificity and fibrinolytic mode of action, suggesting that it is a novel fibrinolytic enzyme with potential applications in the treatment and prevention of thrombosis.
Abstract sourced from PubMed (NCBI) for the cited record. See the original publication for the authoritative version.
Summary
Developing an effective fibrinolytic drug for treating thrombolysis with minimal undesirable side effects is of great importance.
Why This Matters for Hirudotherapy
This study purified and characterized a novel fibrinolytic enzyme (WPI01, molecular mass 27044.297 Da) from Whitmania pigra that achieved 50.59% blood clot reduction in vitro at 500 U/mL within 6 hours—higher than urokinase at 1000 U/mL—and produced halos on heated and unheated fibrin plates, suggesting both direct fibrin degradation and possible plasminogen activator activity. This is relevant to ASH's domain as the abstract states WPI01 has potential applications in the treatment and prevention of thrombosis and is a novel fibrinolytic enzyme derived from a leech species. The characterization is entirely in vitro, with no animal or clinical data presented; therapeutic applicability remains unestablished pending further study.
Citation
Purification and characterization of a novel fibrinolytic enzyme from Whitmania pigra Whitman
Jiang Q et al. · Protein expression and purification, 2020
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