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Please use this identifier to cite or link to this item: http://ir.ncue.edu.tw/ir/handle/987654321/16768

Title: Cloning and Expression of a cDNA Coding for Catalase from Zebrafish (Danio rerio)
Authors: Ken, Chuian-Fu;Lin, Chi-Tsai;Wu, Jen-Leih;Shaw, Jei-Fu
Contributors: 生物學系
Keywords: Zebrafish;Danio rerio;Molecular cloning;cDNA;Catalase;Expression;Escherichia coli;RACE-PCR;pET-20b(+)
Date: 2000-06
Issue Date: 2013-06-05T08:48:08Z
Publisher: American Chemical Society
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.
Relation: Journal of Agricultural and Food Chemistry, 48(6): 2092-2096
Appears in Collections:[生物學系] 期刊論文

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