Two peroxidases isolated from kidney bean cell suspension cultures

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Abstract
Two peroxidases, isolated from filtrates of suspension cultures of a cell line derived from red kidney bean (Phaseolus vulgaris) were purified 145- and 72-fold respectively. The two enzymes were quite similar in many of their properties and both were typical plant peroxidases. They differed markedly, however, in their molecular weights (estimated by gel filtration). The molecular weight of peroxidase I was 30 000 whereas that of peroxidase II was only 6000.
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