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Research Project: MOLECULAR ANALYSIS OF VIRULENCE DETERMINANTS OF SELECT BACTERIA IN FISH DISEASES

Location: Aquatic Animal Health Research

Title: Channel catfish, Ictalurus punctatus, myeloperoxidase cDNA

Authors

Submitted to: Genbank
Publication Type: Other
Publication Acceptance Date: September 2, 2009
Publication Date: September 2, 2009
Citation: Yeh, H., Klesius, P.H. 2009. Channel catfish, Ictalurus punctatus, myeloperoxidase cDNA. Genbank. Accession No. G2429001.

Technical Abstract: Myeloperoxidase (EC 1.11.1.7), a heme-containing lysosomal glycoprotein, is found in azurophilic granules of neutrophils and monocytes. Upon activation, neutrophiles produce hydrogen peroxide and release myeloperoxidase from the granules that the latter catalyzes the former in the presence of various halide ions to form hypohalous acids. Subsequently, these reagents are able to kill the invading microorganisms. In this communication, we identified and characterized the channel catfish myeloperoxidase transcript. The full-length nucleotide sequence of channel catfish myeloperoxidase cDNA comprised of 3157 nucleotides, including an open reading frame, which appears to encode a putative peptide of 771 amino acid residues with a calculated molecular mass of 87.14 kDa. By comparison with human counterpart, the channel catfish myeloperoxidase peptide can be divided into domains, and has conservative features. This result provides important information for further elucidating myeloperoxidase in channel catfish.

   

 
Project Team
Pridgeon, Yuping - Julia
Yeh, Hung-Yueh
 
Publications
   Publications
 
Related National Programs
  Aquaculture (106)
 
 
Last Modified: 05/23/2013
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