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Please use this identifier to cite or link to this item: http://ntour.ntou.edu.tw:8080/ir/handle/987654321/45593

Title: Cloning and expression of a cDNA coding for catalase from zebrafish (Danio rerio)
Authors: Chuian-Fu Ken
Chi-Tsai Lin
Jen-Leih Wu
Jei-Fu Shaw
Contributors: 國立臺灣海洋大學:生命科學系
Keywords: pET-20b(+)
Danio rerio
Zebrafish
molecular cloning
cDNA
catalase
expression
Escherichia coli
RACE−PCR
Date: 2000
Issue Date: 2018-03-28T01:23:17Z
Publisher: Journal of Agricultural and Food Chemistry
Abstract: 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 zebrafish (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.
Relation: 48(6)
URI: http://ntour.ntou.edu.tw:8080/ir/handle/987654321/45593
Appears in Collections:[生命科學系] 期刊論文

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