<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Qiao K</submitter><funding>the National Key Research and Development Program of China</funding><pagination>3071</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC8954737</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>23(6)</volume><pubmed_abstract>Pufferfish are considered a culinary delicacy but require careful preparation to avoid ingestion of the highly toxic tetrodotoxin (TTX), which accumulates in certain tissues. In this study, the tissue distribution of peroxiredoxin-1 from Takifugu bimaculatus was investigated. The peroxiredoxin-1 protein was obtained by in vitro recombinant expression and purification. The recombinant protein had a strong ability to scavenge hydroxyl radicals, protect superhelical DNA plasmids from oxidative damage, and protect L929 cells from H2O2 toxicity through in vitro antioxidant activity. In addition, we verified its ability to bind to tetrodotoxin using surface plasmon resonance techniques. Further, recombinant proteins were found to facilitate the entry of tetrodotoxin into cells. Through these ana</pubmed_abstract><journal>International journal of molecular sciences</journal><pubmed_title>Molecular Characterization of a New Tetrodotoxin-Binding Protein, Peroxiredoxin-1, from Takifugu bimaculatus.</pubmed_title><pmcid>PMC8954737</pmcid><funding_grant_id>2018YFD0901102</funding_grant_id><funding_grant_id>2020R1013008</funding_grant_id><funding_grant_id>in 2021</funding_grant_id><pubmed_authors>Liu Z</pubmed_authors><pubmed_authors>Xu M</pubmed_authors><pubmed_authors>Wang C</pubmed_authors><pubmed_authors>Feng H</pubmed_authors><pubmed_authors>Huang L</pubmed_authors><pubmed_authors>Liu S</pubmed_authors><pubmed_authors>Su J</pubmed_authors><pubmed_authors>Qiao K</pubmed_authors><pubmed_authors>Su Y</pubmed_authors><pubmed_authors>Chen B</pubmed_authors><pubmed_authors>Pan N</pubmed_authors></additional><is_claimable>false</is_claimable><name>Molecular Characterization of a New Tetrodotoxin-Binding Protein, Peroxiredoxin-1, from Takifugu bimaculatus.</name><description>Pufferfish are considered a culinary delicacy but require careful preparation to avoid ingestion of the highly toxic tetrodotoxin (TTX), which accumulates in certain tissues. In this study, the tissue distribution of peroxiredoxin-1 from Takifugu bimaculatus was investigated. The peroxiredoxin-1 protein was obtained by in vitro recombinant expression and purification. The recombinant protein had a strong ability to scavenge hydroxyl radicals, protect superhelical DNA plasmids from oxidative damage, and protect L929 cells from H2O2 toxicity through in vitro antioxidant activity. In addition, we verified its ability to bind to tetrodotoxin using surface plasmon resonance techniques. Further, recombinant proteins were found to facilitate the entry of tetrodotoxin into cells. Through these ana</description><dates><release>2022-01-01T00:00:00Z</release><publication>2022 Mar</publication><modification>2025-04-04T22:13:42.513Z</modification><creation>2025-04-04T22:13:42.513Z</creation></dates><accession>S-EPMC8954737</accession><cross_references><pubmed>35328490</pubmed><doi>10.3390/ijms23063071</doi></cross_references></HashMap>