[On characterization of lipoxygenase from barley (author's transl)].
Lipoxygenase from brewing barley of Nordbaden has optimum activity at alkaline pH and predominantly forms 9-hydroperoxy-10-trans, 12-cis-octadecadienoic acid (9-LHPO) from linoleic acid. While at pH 7 90% 9-LHPO is produced, its proportions drops during incubation at more alkaline pH (pH 7,75) to 70%. This positional specifity is not caused by isoenzymes. While linoleic acid methylester is converted only to a lesser degree, trilinolein is not accepted as substrate.
D002374:Catalase / Q000302:isolation & purification; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D002523:Edible Grain / Q000201:enzymology*; D001467:Hordeum / Q000201:enzymology*; D006863:Hydrogen-Ion Concentration; D007527:Isoenzymes / Q000302:isolation & purification; D008084:Lipoxygenase / Q000302:isolation & purification*; D010544:Peroxidases / Q000302:isolation & purification; D011048:Polarography
D007527:Isoenzymes; D010544:Peroxidases; D002374:Catalase; D008084:Lipoxygenase
Zur Charakterisierung der Lipoxygenase aus Gerste.