Endonuclease activity of phenol oxidase from Musca domestica larvae

Sun, S.; Liu, W.; Wang, J.; Yang, S.; Gu, L.; Hong, Y.; Shang, D.; Wang, B.; Su, X.; Qi, S.

Biological Bulletin 215(1): 108-114

2008


ISSN/ISBN: 0006-3185
PMID: 18723642
DOI: 10.2307/25470688
Accession: 031236704

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Abstract
Phenol oxidase (PO), a copper-containing enzyme with oxygenase activity, can convert mono- or diphenol into quinone and plays an important role in the arthropod melanization reaction. Here, we report a new property of PO from Musca domestica larvae: a thermotolerant endonuclease activity, by which PO can degrade plasmid DNA even after being heated to 80 degrees C for 20 min. We cloned PO cDNA, constructed the expression vector pVAX1-PO, and expressed it in HeLa cells.