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.
Resumen
Developing an effective fibrinolytic drug for treating thrombolysis with minimal undesirable side effects is of great importance.
Por qué esto importa para la hirudoterapia
Este estudio purificó y caracterizó una nueva enzima fibrinolítica (WPI01, masa molecular de 27044.297 Da) aislada de Whitmania pigra, que alcanzó una reducción del coágulo sanguíneo del 50.59 % in vitro a 500 U/mL en 6 horas —superior a la uroquinasa a 1000 U/mL— y produjo halos en placas de fibrina calentadas y sin calentar, lo que sugiere tanto degradación directa de fibrina como una posible actividad activadora del plasminógeno. Esto es pertinente para el ámbito de la ASH, ya que el resumen indica que la WPI01 tiene aplicaciones potenciales en el tratamiento y la prevención de la trombosis y constituye una nueva enzima fibrinolítica derivada de una especie de sanguijuela. La caracterización es completamente in vitro, sin que se presenten datos animales ni clínicos; la aplicabilidad terapéutica continúa sin establecerse en espera de nuevos estudios.
Citación
Purification and characterization of a novel fibrinolytic enzyme from Whitmania pigra Whitman
Jiang Q et al. · Protein expression and purification, 2020
Contexto clínico relacionado
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Añadido a la biblioteca ASH: May 27, 2026 · Última actualización del sitio: 18 de junio de 2026