| 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 | | |
Similar Items
| Find | | DEBUG INFO
| | | | TEI-XML for
| default:Reihe_C/36/ZNC-1981-36c-0400.pdf | | | Identifier
| ZNC-1981-36c-0400 | | | Volume
| 36 | |
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 | | |
Similar Items
| Find | | DEBUG INFO
| | | | TEI-XML for
| default:Reihe_C/44/ZNC-1989-44c-0931.pdf | | | Identifier
| ZNC-1989-44c-0931 | | | Volume
| 44 | |
|