Bdellastasin, a serine protease inhibitor of the antistasin family from the medical leech
Biochemistry study published in European Journal of Biochemistry (1998)
Abstract
We have reported earlier the isolation and amino acid composition of bdellin A from medical leech, and characterised it as an inhibitor of trypsin, plasmin and acrosin [Fritz, H., Gebhardt, M., Meister, R. & Fink, E. (1971) in Proceedings of the international research conference on proteinase inhibitors (Fritz, H. & Tschesche, H., eds) pp. 271-280, Walter de Gruyter, Berlin]. In the present study, one of several chromatographic forms of this inhibitor was isolated from a semi-pure preparation. Elucidation of its amino acid sequence revealed that bdellin A is a member of the antistasin family. Therefore, it was renamed bdellastasin to avoid confusion with bdellin B, which is another trypsin-plasmin inhibitor from the medical leech, but of the Kazal type. Furthermore, a synthetic gene of bdellastasin was constructed, and the protein expressed in Saccharomyces cerevisiae with yields of 29 mg/l. The recombinant bdellastasin was purified by hydrophobic interaction and anion-exchange chromatography. Comparison by mass spectroscopy, far-ultraviolet circular dichroism studies, sequence determination, and inhibition characteristics demonstrated the identity of recombinant and native bdellastasin. The Ki values of bdellastasin for inhibition of bovine trypsin and human plasmin are in the nanomolar range; no inhibition was detected for factor Xa, thrombin, tissue kallikrein, plasma kallikrein and chymotrypsin. Circular dichroism analyses indicated that bdellastasin is devoid of secondary-structural elements.
Abstract sourced from PubMed (NCBI) for the cited record. See the original publication for the authoritative version.
Resumen
First isolation and characterization of bdellastasin from Hirudo medicinalis — antistasin-family inhibitor expressed in yeast for structural and functional studies.
Por qué esto importa para la hirudoterapia
Este estudio aisló una forma cromatográfica de bdellina A de la sanguijuela medicinal, determinó su secuencia de aminoácidos y la renombró como bdellastasina al confirmar su pertenencia a la familia de las antiestatinas. Un gen sintético de bdellastasina se expresó en Saccharomyces cerevisiae a 29 mg/L, y se demostró que la proteína recombinante era idéntica a la bdellastasina nativa mediante espectrometría de masas, dicroísmo circular, secuenciación y perfil de inhibición. La bdellastasina inhibe la tripsina bovina y la plasmina humana con valores de Ki en el rango nanomolar, pero no muestra inhibición del factor Xa, la trombina, la calicreína tisular o plasmática ni la quimotripsina, y el dicroísmo circular indica ausencia de estructura secundaria regular. Esto es relevante para la ASH como caracterización molecular de un componente del secretoma de la sanguijuela medicinal con expresión recombinante establecida. El estudio se limita a la caracterización bioquímica; no se reportan datos in vivo ni clínicos.
Citación
Bdellastasin, a serine protease inhibitor of the antistasin family from the medical leech.
Moser M et al. · European journal of biochemistry, 1998
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Añadido a la biblioteca ASH: May 27, 2026 · Última actualización del sitio: 18 de junio de 2026