Literature DB >> 7696305

Peroxidase activity in the ink gland of Sepia officinalis and partial nucleotide sequence of a candidate cDNA encoding the enzyme.

A Palumbo1, I J Jackson.   

Abstract

A peroxidase was partially purified from the ink gland of the cuttlefish Sepia officinalis. This enzyme acts on guaiacol and I- as substrates and is inhibited by cyanide and azide. By using the PCR technique we have isolated and sequenced a cDNA clone encoding a protein homologous to other animal peroxidases. These results are discussed in relation to the possible involvement of peroxidase in the biosynthesis of melanin.

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Year:  1995        PMID: 7696305     DOI: 10.1016/0167-4838(94)00221-2

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN: 0006-3002


  2 in total

1.  Subcellular localization and function of melanogenic enzymes in the ink gland of Sepia officinalis.

Authors:  A Palumbo; A di Cosmo; I Gesualdo; V J Hearing
Journal:  Biochem J       Date:  1997-05-01       Impact factor: 3.857

2.  A peroxidase related to the mammalian antimicrobial protein myeloperoxidase in the Euprymna-Vibrio mutualism.

Authors:  V M Weis; A L Small; M J McFall-Ngai
Journal:  Proc Natl Acad Sci U S A       Date:  1996-11-26       Impact factor: 11.205

  2 in total

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