Peroxidase activity in the ink gland of Sepia officinalis and partial nucleotide sequence of a candidate cDNA encoding the enzyme.
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.
Palumbo
A
A
Zoological Station, Naples, Italy.
Jackson
I J
IJ
D000595:Amino Acid Sequence; D000818:Animals; D018076:DNA, Complementary / Q000302:isolation & purification*; D008969:Molecular Sequence Data; D008974:Mollusca / Q000201:enzymology*; D009195:Peroxidase / Q000235:genetics / Q000302:isolation & purification*
D018076:DNA, Complementary; D009195:Peroxidase