Characterization, molecular modelling and developmental expression of zebrafish manganese superoxide dismutase

Chi Tsai Lin, Wen Chung Tseng, Nai Wan Hsiao, Hsiao Huang Chang, Chuian Fu Ken

Research output: Contribution to journalArticle

30 Citations (Scopus)

Abstract

A 977 bp cDNA containing an open reading frame encoding 224 amino acid residues of manganese superoxide dismutase was cloned from zebrafish (zMn-SOD). The deduced amino acid sequence showed high identity with the sequences of Mn-SODs from human (85.1%) to nematode (61.6%). The 3-D structure model was superimposed on the relative domains of human Mn-SOD with the root mean square (rms) deviation of 0.0919 Å. The recombinant mature zMn-SOD with enzyme activity was purified using His-tag technique. The half-life of the enzyme is approximately 48 min and its thermal inactivation rate constant kd is 0.0154 min-1at 70 °C. The enzyme was active under a broad pH (2.2-11.2) and in the presence of up to 4% SDS. Real-time RT-PCR assay was used to detect the zMn-SOD mRNA expression during the developmental stages following a challenge with paraquat. A high level expression of Mn-SOD mRNA was detected at the cleavage stage, but decreased significantly under paraquat treatment. The results indicated that Mn-SOD plays an important role during embryonic development.

Original languageEnglish
Pages (from-to)318-324
Number of pages7
JournalFish and Shellfish Immunology
Volume27
Issue number2
DOIs
Publication statusPublished - 2009 Aug

Fingerprint

paraquat
Molecular modeling
Danio rerio
Superoxide Dismutase
manganese
superoxide dismutase
amino acid
enzyme
embryonic development
developmental stage
Paraquat
half life
cleavage
modeling
enzyme activity
nematode
assay
Amino Acids
Messenger RNA
Enzyme activity

All Science Journal Classification (ASJC) codes

  • Environmental Chemistry
  • Aquatic Science

Cite this

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title = "Characterization, molecular modelling and developmental expression of zebrafish manganese superoxide dismutase",
abstract = "A 977 bp cDNA containing an open reading frame encoding 224 amino acid residues of manganese superoxide dismutase was cloned from zebrafish (zMn-SOD). The deduced amino acid sequence showed high identity with the sequences of Mn-SODs from human (85.1{\%}) to nematode (61.6{\%}). The 3-D structure model was superimposed on the relative domains of human Mn-SOD with the root mean square (rms) deviation of 0.0919 {\AA}. The recombinant mature zMn-SOD with enzyme activity was purified using His-tag technique. The half-life of the enzyme is approximately 48 min and its thermal inactivation rate constant kd is 0.0154 min-1at 70 °C. The enzyme was active under a broad pH (2.2-11.2) and in the presence of up to 4{\%} SDS. Real-time RT-PCR assay was used to detect the zMn-SOD mRNA expression during the developmental stages following a challenge with paraquat. A high level expression of Mn-SOD mRNA was detected at the cleavage stage, but decreased significantly under paraquat treatment. The results indicated that Mn-SOD plays an important role during embryonic development.",
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Characterization, molecular modelling and developmental expression of zebrafish manganese superoxide dismutase. / Lin, Chi Tsai; Tseng, Wen Chung; Hsiao, Nai Wan; Chang, Hsiao Huang; Ken, Chuian Fu.

In: Fish and Shellfish Immunology, Vol. 27, No. 2, 08.2009, p. 318-324.

Research output: Contribution to journalArticle

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