Shechter G, Grossman S
Int J Biochem. 1983;15(11):1295-304. doi: 10.1016/0020-711x(83)90019-8.
Lipoxygenase activity was extracted from the mitochondrial fraction of baker's yeast and was purified by affinity chromatography on a linoleyl aminoethyl sepharose column. Two lipoxygenases were eluted from the affinity column. The second enzyme eluted was characterized as a true lipoxygenase. The lipoxygenase eluted showed maximum activity at pH 6.5 with a Km of 2.68 X 10(-4) M on linoleate. The reaction products of the second lipoxygenase with linoleate were characterized by u.v., i.r., NMR spectra and mass spectrometry and were found to be: 9-hydroperoxy-octadeca-trans-10,cis-12-dienoic acid and 13-hydroperoxy-octadeca-cis-9,trans-11-dienoic acid.
脂氧合酶活性从面包酵母的线粒体部分提取，并通过在亚油酰氨乙基琼脂糖柱上进行亲和层析进行纯化。从亲和柱上洗脱下来两种脂氧合酶。洗脱下来的第二种酶被鉴定为真正的脂氧合酶。洗脱下来的脂氧合酶在pH 6.5时表现出最大活性，对亚油酸的Km值为2.68×10⁻⁴ M。第二种脂氧合酶与亚油酸的反应产物通过紫外、红外、核磁共振光谱和质谱进行表征，结果发现是：9-氢过氧-十八碳-反式-10,顺式-12-二烯酸和13-氢过氧-十八碳-顺式-9,反式-11-二烯酸。
