PUBLICATION
Purification and characterization of glutathione peroxidase 1 in the red muscle of Pacific bluefin tuna Thunnus orientalis
- Authors
- Yamashita, Y., Yabu, T., Touhata, K., and Yamashita, M.
- ID
- ZDB-PUB-180820-27
- Date
- 2012
- Source
- Fisheries science : FS 78: 407-413 (Journal)
- Registered Authors
- Yamashita, Michiaki
- Keywords
- Pacific bluefin tuna, Fish, Glutathione peroxidase, Red muscle, Selenium, Selenoprotein
- MeSH Terms
- none
- PubMed
- none Full text @ Fisheries Science
Citation
Yamashita, Y., Yabu, T., Touhata, K., and Yamashita, M. (2012) Purification and characterization of glutathione peroxidase 1 in the red muscle of Pacific bluefin tuna Thunnus orientalis. Fisheries science : FS. 78:407-413.
Abstract
Glutathione peroxidase GPx1 was purified from the red muscle of Pacific bluefin tuna Thunnus orientalis and its enzymatic properties were characterized. The enzyme was optimally active at pH 7.4 with a specific activity for hydrogen peroxide and a K m of 6.7 μM. cDNA was also isolated and it contained a predicted open reading frame (ORF) encoding a 188 amino acid protein. The phylogenetic tree shows that fish including Pacific bluefin tuna, pufferfish, and zebrafish, but not mammals, possess two genetically distinct types of GPx1, i.e., GPx1a and GPx1b. The purified enzyme was classified as a fish GPx-1b enzyme on the basis of the phylogenetic tree of the GPx1 family.
Genes / Markers
Expression
Phenotype
Mutations / Transgenics
Human Disease / Model
Sequence Targeting Reagents
Fish
Orthology
Engineered Foreign Genes
Mapping