| Literature DB >> 1548473 |
M Nishiyama1, H Okamoto, T Watanabe, T Hori, T Hada, N Ueda, S Yamamoto, H Tsukamoto, K Watanabe, T Kirino.
Abstract
The cytosol fraction from a thoroughly irrigated canine cerebrum was subjected to immunoaffinity chromatography using a monoclonal antibody against porcine leukocyte 12-lipoxygenase. Arachidonate 12-lipoxygenase eluted from the column with some retardation. The enzyme, with a specific activity of 9 nmol/min/mg of protein, converted arachidonic acid to 12(S)-hydroperoxy-5,8,10,14-eicosatetraenoic acid. The enzyme was active not only with arachidonic acid, but also with linoleic and alpha-linolenic acids. In contrast, 12-lipoxygenase of canine platelets was almost inactive with linoleic and alpha-linolenic acids, and the platelet enzyme was also distinguished from the cerebral enzyme in terms of reactivity with the anti-12-lipoxygenase antibody. 12-Lipoxygenase activity was also detected in the cytosol fractions of other parts of canine brain: basal ganglia, hippocampus, cerebellum, olfactory bulb, and medulla oblongata.Entities:
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Year: 1992 PMID： 1548473 DOI： 10.1111/j.1471-4159.1992.tb11355.x
Source DB: PubMed Journal: J Neurochem ISSN： 0022-3042 Impact factor: 5.372