ZfN: Search Results

1	Author	Toshihisa Ohshima, Gerhart Drews	Requires 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

2	Author	P. Eter Proksch, M. Argareta Proksch, W. Altraud Weck, Eloy Rodriguez	Requires 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

3	Author	Dieter Strack, Jürgen Heilemann, Eva-Susan Klinkott, Victor Wray	Requires 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

4	Author	Ralf Perrey, Marie-Theres Hauser, MichaelW. Ink	Requires 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