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Heligmosomoides polygyrus: peroxidase activity
Authors:C M Preston  J Barrett
Institution:1. Institute of Wood Technology and Renewable Materials, Department of Material Sciences and Process Engineering, BOKU - University of Natural Resources and Life Sciences, Vienna, Konrad-Lorenz-Strasse 24, 3430, Tulln, Austria;2. Institute of Microbial Genetics (IMiG), Department of Applied Genetics and Cell Biology, BOKU - University of Natural Resources and Life Sciences, Vienna, Konrad-Lorenz-Strasse 24, 3430, Tulln, Austria;3. Institute of Environmental Biotechnology, Department of Agrobiotechnology, IFA-Tulln, BOKU - University of Natural Resources and Life Sciences, Vienna, Konrad-Lorenz-Strasse 20, 3430, Tulln, Austria;4. Institute of Biotechnology in Plant Production, Department of Crop Sciences, BOKU - University of Natural Resources and Life Sciences, Vienna, Konrad-Lorenz-Strasse 20, 3430, Tulln, Austria;1. International Flavors & Fragrances, Larkin Laboratory, 1803 Larkin Center Drive, Midland, MI, 48642, USA;2. Charles River (CR-MWN), 54943 N. Main Street, Mattawan, MI, 49071, USA;3. Labcorp Drug Development, 671 South Meridian Road, Greenfield, IN, 46140, USA;4. DuPont Stine-Haskell, 1090 Elkton Rd, Newark, DE, 19714, USA;5. Teva Pharmaceuticals, 145 Brandywine Parkway, West Chester, PA, 19380, USA;6. International Flavors & Fragrances, Leiden Bio Science Park, Galileiweg 8, 2333 BD, Leiden, the Netherlands;7. Benson Hill, 1001 N Warson Rd, St. Louis, MO, 63132, USA;8. International Flavors & Fragrances, 3329 Agriculture Drive, Madison, WI, 53716, USA;9. International Flavors & Fragrances, Health & Biosciences Danisco Sweeteners Oy, Sokeritehtaantie 20, 02460, Kantvik, Finland;10. International Flavors & Fragrances, Health & Biosciences, c/o Danisco UK Ltd., Reigate, RH2 9PW, United Kingdom;11. International Flavors & Fragrances, DuPont Experimental Station, Bldg. 353, 200 Powder Mill Rd, Wilmington, DE, 19803, USA;1. Guangzhou Institute of Geography, Guangdong Academy of Sciences, Guangzhou, China;2. School of Geography and Planning, Sun Yat-sen University, Guangzhou, China
Abstract:Peroxidase activity in Heligmosomoides polygyrus was located primarily in the mitochondrion. The enzyme was active with a range of organic and inorganic electron donors and, in addition to hydrogen peroxide, it could utilize cumene peroxide, but the highest activity was obtained with linoleic acid peroxide. The effects of electron chain substrates and inhibitors on H. polygyrus mitochondrial peroxidase activity was consistent with the enzyme being linked functionally to cytochrome c, although in vivo, this may not be the only electron donor. The interaction of the peroxidase with electron transport is discussed.
Keywords:
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