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...

Descripción completa

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
_version_ 1784898021988761600
author Yap, Wei Yuen
Loo, Lok Wenn
Sha, Hong Xi
Hwang, Jung Shan
author_facet Yap, Wei Yuen
Loo, Lok Wenn
Sha, Hong Xi
Hwang, Jung Shan
author_sort Yap, Wei Yuen
collection PubMed
description 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.
format Online
Article
Text
id pubmed-9971028
institution National Center for Biotechnology Information
language English
publishDate 2023
publisher Elsevier
record_format MEDLINE/PubMed
spelling pubmed-99710282023-03-01 Enhanced production of recombinant HALT-1 pore-forming toxin using two-step chromatographic procedure Yap, Wei Yuen Loo, Lok Wenn Sha, Hong Xi Hwang, Jung Shan MethodsX Method Article 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. Elsevier 2023-02-11 /pmc/articles/PMC9971028/ /pubmed/36865650 http://dx.doi.org/10.1016/j.mex.2023.102073 Text en © 2023 The Author(s) https://creativecommons.org/licenses/by/4.0/This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Method Article
Yap, Wei Yuen
Loo, Lok Wenn
Sha, Hong Xi
Hwang, Jung Shan
Enhanced production of recombinant HALT-1 pore-forming toxin using two-step chromatographic procedure
title Enhanced production of recombinant HALT-1 pore-forming toxin using two-step chromatographic procedure
title_full Enhanced production of recombinant HALT-1 pore-forming toxin using two-step chromatographic procedure
title_fullStr Enhanced production of recombinant HALT-1 pore-forming toxin using two-step chromatographic procedure
title_full_unstemmed Enhanced production of recombinant HALT-1 pore-forming toxin using two-step chromatographic procedure
title_short Enhanced production of recombinant HALT-1 pore-forming toxin using two-step chromatographic procedure
title_sort enhanced production of recombinant halt-1 pore-forming toxin using two-step chromatographic procedure
topic Method Article
url 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
work_keys_str_mv AT yapweiyuen enhancedproductionofrecombinanthalt1poreformingtoxinusingtwostepchromatographicprocedure
AT loolokwenn enhancedproductionofrecombinanthalt1poreformingtoxinusingtwostepchromatographicprocedure
AT shahongxi enhancedproductionofrecombinanthalt1poreformingtoxinusingtwostepchromatographicprocedure
AT hwangjungshan enhancedproductionofrecombinanthalt1poreformingtoxinusingtwostepchromatographicprocedure

Ejemplares similares