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NADH-Ferricyanide Reductase of Leaf Plasma Membranes: Partial Purification and Immunological Relation to Potato Tuber Microsomal NADH-Ferricyanide Reductase and Spinach Leaf NADH-Nitrate Reductase
Högskolan i Jönköping, Högskolan för lärande och kommunikation, HLK, Ämnesforskning. Department of Plant Biochemistry, University of Lund, Lund, Sweden.ORCID-id: 0000-0003-0117-2974
Laboratoire de Biomembranes Vegetales, Unité de Recherche Associé 1180, Université Pierre et Marie Curie, Paris, France.
Faculty of Horticulture, Chiba University, Matsudo, Chiba, Japan.
Laboratoire de Biomembranes Vegetales, Unité de Recherche Associé 1180, Université Pierre et Marie Curie, Paris, France.
1991 (engelsk)Inngår i: Plant Physiology, ISSN 0032-0889, E-ISSN 1532-2548, Vol. 95, nr 1, s. 6-13Artikkel i tidsskrift (Fagfellevurdert) Published
Abstract [en]

Plasma membranes obtained by two-phase partitioning of microsomal fractions from spinach (Spinacea oleracea L. cv Medania) and sugar beet leaves (Beta vulgaris L.) contained relatively high NADH-ferricyanide reductase and NADH-nitrate reductase (NR; EC 1.6.6.1) activities. Both of these activities were latent. To investigate whether these activities were due to the same enzyme, plasma membrane polypeptides were separated with SDS-PAGE and analyzed with immunoblotting methods. Antibodies raised against microsomal NADH-ferricyanide reductase (tentatively identified as NADH-cytochrome b5 reductase, EC 1.6.2.2), purified from potato (Solanum tuberosum L. cv Bintje) tuber microsomes, displayed one single band at 43 kilodaltons when reacted with spinach plasma membranes, whereas lgG produced against NR from spinach leaves gave a major band at 110 kilodaltons together with a few fainter bands of lower molecular mass. Immunoblotting analysis using inside-out and right-side-out plasma membrane vesicles strongly indicated that NR was not an integral protein but probably trapped inside the plasma membrane vesicles during homogenization. Proteins from spinach plasma membranes were solubilized with the zwitterionic detergent 3-[(3-cholamidopropyl) dimethylammonio] 1-propane-sulfonate and separated on a Mono Q anion exchange column at pH 5.6 with fast protein liquid chromatography. One major peak of NADH-ferricyanide reductase activity was found after separation. The peak fraction was enriched about 70-fold in this activity compared to the plasma membrane. When the peak fractions were analyzed with SDS-PAGE the NADH-ferricyanide reductase activity strongly correlated with a 43 kilodalton polypeptide which reacted with the antibodies against potato microsomal NADH-ferricyanide reductase. Thus, our data indicate that most, if not all, of the truly membrane-bound NADH-ferricyanide reductase activity of leaf plasma membranes is due to an enzyme very similar to potato tuber microsomal NADH-ferricyanide reductase (NADH-cytochrome b5 reductase).

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1991. Vol. 95, nr 1, s. 6-13
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URN: urn:nbn:se:hj:diva-2180PubMedID: 16667982OAI: oai:DiVA.org:hj-2180DiVA, id: diva2:33000
Tilgjengelig fra: 2007-10-17 Laget: 2007-10-17 Sist oppdatert: 2017-12-12bibliografisk kontrollert

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