Enhanced production of recombinant HALT-1 pore-forming toxin using two-step chromatographic procedure

Hydra actinoporin-like toxin-1 (HALT-1) has been isolated from Hydra magnipapillata and is highly cytolytic against various human cells including erythrocyte. Previously, recombinant HALT-1 (rHALT-1) was expressed in Escherichia coli • HALT-1 is a soluble α-pore-forming toxin of 18.38 kDa. • rHALT-1...

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Detalles Bibliográficos
Autores principales: Yap, Wei Yuen, Loo, Lok Wenn, Sha, Hong Xi, Hwang, Jung Shan
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier 2023
Materias:
Method Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9971028/
https://www.ncbi.nlm.nih.gov/pubmed/36865650
http://dx.doi.org/10.1016/j.mex.2023.102073
Descripción
Sumario:Hydra actinoporin-like toxin-1 (HALT-1) has been isolated from Hydra magnipapillata and is highly cytolytic against various human cells including erythrocyte. Previously, recombinant HALT-1 (rHALT-1) was expressed in Escherichia coli • HALT-1 is a soluble α-pore-forming toxin of 18.38 kDa. • rHALT-1 was purified by nickel affinity chromatography followed by SP cation exchange chromatography. • The cytotoxicity of purified rHALT-1 using 2-step purifications via either phosphate or acetate buffer was comparable to those previously reported.

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