A study of lipoxidase in pea seeds and seedlings

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Abstract
Lipoxidase enzyme was isolated and partly purified from pea seeds by ultracentrifugation, ammonium sulphate precipitation, Sephadex and DEAE‐Cellulose column chromatography. The pH optimum of the enzyme was 7.2 and the Michaelis–Menton constant 2.3 × 10−3 M. Disc gel electrophoresis revealed the presence of 3 to 4 isoenzymes, while the molecular weight determination in the presence of sodium dodecyl sulphate gave a value of 7.4 × 104. The presence of lipoxidase in pea mitochondria and in the peroxisome‐like bodies was demonstrated. A low enzyme activity was found with the purified chloroplasts but a much higher activity was found in the plastids and in the cytoplasm of the etiolated tissue. The enzyme was found not to be compartmentalised in any particulate fraction of the pea seedlings investigated.