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1989 (1)
1988 (1)
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1981 (1)
1Author    Toshihisa Ohshima, Gerhart DrewsRequires cookie*
 Title    Isolation and Partial Characterization of the Membrane-Bound NADH Dehydrogenase from the Phototrophic Bacterium Rhodopseudomonas capsulata  
 Abstract    Chem otrophically grown cells of Rhodopseudomonas capsulata contain at least three different pyridine nucleotide dehydrogenases, i) a soluble, found in the supernatant (144000 x g) o f cell free extracts, N AD H-dependent, ii) a mem brane-bound, N AD H -dependent, and iii) a soluble, found in the supernatant N AD PH dependent. i The m em brane-bound N A D H dehydrogenase (E.C. 1.6.99.3) has been solubilized by sodium deoxycholate treatm ent of m em branes and purified 75 fold by column chrom atography on Sephadex G-150 and DEAE cellulose in the presence of sodium cholate. The native enzyme has an apparent molecular mass (M r) o f 97 000, containing polypeptides of Mr of about 15 000. The pH optim um was at 7.5. The enzyme was specific for NADH. The Michaelis constant for NADH and DCIP were 4.0 and 63 hm, respectively. The enzyme was inactivated by FM N, riboflavin and NADH. In contrast, the soluble N ADH-dehydrogenase (i) was activated by FMN. 
  Reference    Z. Naturforsch. 36c, 400 (1981); received February 23/M arch 16 1981 
  Published    1981 
  Keywords    NADH Dehydrogenase, Purification, Localization, Inhibitors, Rhodopseudomonas capsulata 
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 TEI-XML for    default:Reihe_C/36/ZNC-1981-36c-0400.pdf 
 Identifier    ZNC-1981-36c-0400 
 Volume    36 
2Author    P. Eter Proksch, M. Argareta Proksch, W. Altraud Weck, Eloy RodriguezRequires cookie*
 Title    Localization of Chromenes and Benzofurans in the Genus Encelia (Asteraceae)  
 Abstract    Phytochemical and microscopial analysis of leaves and stems of various species of Encelia showed a strict correlation between the presence of resin ducts and the accumulation of benzopy­ rans and benzofurans. Fluorescence microscopy of Encelia farinosa proved unambigously that these compounds are stored exclusivly in the resin ducts and the surrounding cells. 
  Reference    Z. Naturforsch. 40c, 301 (1985); received December 18 1984 
  Published    1985 
  Keywords    Encelia, Asteraceae, Benzofurans and Benzopyrans, Localization, Resin Ducts 
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 TEI-XML for    default:Reihe_C/40/ZNC-1985-40c-0301.pdf 
 Identifier    ZNC-1985-40c-0301 
 Volume    40 
3Author    Dieter Strack, Jürgen Heilemann, Eva-Susan Klinkott, Victor WrayRequires cookie*
 Title    Cell Wall-Bound Phenolics from Norway Spruce (Picea abies) Needles  
 Abstract    Insoluble phenolics have been isolated and identified from Norway spruce (Picea abies [L.] KARST.) needles as cell wall-bound astragalin (kaempferol 3-O-ß-glucoside) and p-coumaric acid as major components, and ferulic acid as a minor one. They probably mainly occur as lignin-carbohydrate complexes. 
  Reference    Z. Naturforsch. 43c, 37—41 (1988); received August 25 1987 
  Published    1988 
  Keywords    Picea abies (L) KARST, Hydroxycinnamic Acids, Flavonols, Cell Wall, Localization 
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 TEI-XML for    default:Reihe_C/43/ZNC-1988-43c-0037.pdf 
 Identifier    ZNC-1988-43c-0037 
 Volume    43 
4Author    Ralf Perrey, Marie-Theres Hauser, MichaelW. InkRequires cookie*
 Title    Cellular and Subcellular Localization of Peroxidase Isoenzymes in Plants and Cell Suspension Cultures from Lupinus polyphyllus  
 Abstract    , leaf protoplasts and cell suspension cultures of Lupinus polyphyllus and isolated vacuoles were studied for cellular and subcellular localization of peroxidase isoenzymes. Isoelectric focusing revealed 16 peroxidase isoenzymes. The basic peroxidase isoenzymes are predominantly localized in the vacuole and, to a minor degree, unbound in the intercellular space. The acidic isoenzymes are cell wall-bound in plants and not detectable in suspension-cultured cells. Large amounts (up to 11.0 U/ml) of a single basic isoenzyme are detectable in the spent medium of cell suspension cultures. 
  Reference    Z. Naturforsch. 44c, 931—936 (1989); received August 4 1989 
  Published    1989 
  Keywords    Lupinus, Peroxidase, Localization, Isoelectric Focusing (Peroxidase), Cell Culture Leaves, stems, roots 
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 TEI-XML for    default:Reihe_C/44/ZNC-1989-44c-0931.pdf 
 Identifier    ZNC-1989-44c-0931 
 Volume    44