Abstract：
:We have previously reported the purification and partial characterization of two cationic peroxidases from the cell walls of seeds and seedlings of the South American conifer, Araucaria araucana. In this work, we have studied the amino acid composition and NH2-terminal sequences of both enzymes. We also compare the data obtained from these analyses with those reported for other plant peroxidases. The two peroxidases are similar in their amino acid compositions. Both are particularly rich in glycine, which comprises more than 30% of the amino acid residues. The content of serine is also high, ca 17%. The two enzymes are different in their content of arginine, alanine, valine, phenylalanine and threonine. Both peroxidases have identical NH2-terminal sequences, indicating that the two proteins are genetically related and probably are isoforms of the same kind of peroxidase. The amino acid composition and NH2-terminal sequence analyses showed marked differences from the cationic peroxidases from turnip and horseradish.
journal_name
Phytochemistryjournal_title
Phytochemistryauthors
Riquelme A,Cardemil Ldoi
10.1016/0031-9422(94)00665-gsubject
Has Abstractpub_date
1995-05-01 00:00:00pages
29-32issue
1eissn
0031-9422issn
1873-3700pii
003194229400665Gjournal_volume
39pub_type
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