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'Enzyme Purification' in keywords Facet   Publication Year 1987  [X]
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1Author    Pedro Macias, M., Carmen Pinto, JoseE. CampilloRequires cookie*
 Title    Purification and Partial Characterization of Rat Liver Lipoxygenase  
 Abstract    Lipoxygenase was purified from rat liver cytosolic fraction by a method involving two successive chromatographic steps on Sephacryl S-200 and Phenyl Sepharose CL-4B. The enzyme has a molecular weight of 96 Kdal and it seems to be composed of two identical subunits. Chromatofocusing of the enzyme revealed a single band of activity at pi 6.3. The enzyme activity of the purified fraction showed maximum activity at pH 7.0 with a Km for linoleic acid of 1.4 /<M and is competitively inhibited by the specific lipoxygenase inhibitor nordihydroguaiaretic acid. The purified enzyme shows absorption and fluorescence spectra similar to those of lipoxygenase from other sources. However, the molecular weight of lipoxygenase purified from liver is found to be different from that of the enzyme from polymorphonuclear leukocytes. It is suggested that there are different isoenzymes of lipoxygenases in mammals. 
  Reference    Z. Naturforsch. 42b, 1343—1348 (1987); received March 16 1987 
  Published    1987 
  Keywords    Lipoxygenase, Enzyme Purification, Hydrophobic Chromatography 
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 TEI-XML for    default:Reihe_B/42/ZNB-1987-42b-1343.pdf 
 Identifier    ZNB-1987-42b-1343 
 Volume    42