Cloning and expression of a cDNA coding for catalase from zebrafish (Danio rerio)

Chuian Fu Ken, Chi Tsai Lin, Jen Leih Wu, Jei Fu Shaw

Research output: Contribution to journalArticle

18 Citations (Scopus)

Abstract

A full-length complementary DNA (cDNA) clone encoding a catalase was amplified by the rapid amplication of cDNA ends-polymerase chain reaction (RACE-PCR) technique from zebra fish (Danio rerio) mRNA. Nucleotide sequence analysis of this cDNA clone revealed that it comprised a complete open reading frame coding for 526 amino acid residues and that it had a molecular mass of 59 654 Da. The deduced amino acid sequence showed high similarity with the sequences of catalase from swine (86.9%), mouse (85.8%), rat (85%), human (83.7%), fruit fly (75.6%), nematode (71.1%), and yeast (58.6%). The amino acid residues for secondary structures are apparently conserved as they are present in other mammal species. Furthermore, the coding region of zebrafish catalase was introduced into an expression vector, pET-20b(+), and transformed into Escherichia coli expression host BL21(DE3)pLysS. A 60-kDa active catalase protein was expressed and detected by Coomassie blue staining as well as activity staining on polyacrylamide gel followed electrophoresis.

Original languageEnglish
Pages (from-to)2092-2096
Number of pages5
JournalJournal of Agricultural and Food Chemistry
Volume48
Issue number6
DOIs
Publication statusPublished - 2000 Jun 1

All Science Journal Classification (ASJC) codes

  • Chemistry(all)
  • Agricultural and Biological Sciences(all)

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