| | 1 | Author
| Hans-Jürgen Schuetz, H. Elm, Ut Simon | Requires cookie* | | | Title
| Degradation of NAD(H ) by Endogenous Enzymes of Yeasts and Clostridia  | | | | Abstract
| The time courses of degradation of exogenous NAD and NADH (2.5 m M) catalyzed by en dogenous enzymes present in Saccharom yces cerevisiae, Candida utilis, Clostridium spec. La 1, C lostridium kluyveri, and Clostridium sporogenes have been determined. The half lives of the pyridine nucleotides depend extremely on the organism and, for the same organism, on the growth conditions. C. spec. La 1 as well as C. kluyveri possess only negligible enzyme activities for NAD degradation. However, C. sporogenes shows activities leading to half lives of less than 2 h for NAD and 5 h for NADH. At 25 °C half lives in the order of 5 — 17 h have been observed for Candida utilis under different conditions. The half lives of NAD are roughly 5 times higher in the presence of Saccharom yces cerevisiae. | | | |
Reference
| Z. Naturforsch. 41c, 172—178 (1986); received July 25. 1985 | | | |
Published
| 1986 | | | |
Keywords
| NAD(H) Degradation, Clostridia, Yeasts, Bioconversion, Enzymatic Reductions | | | |
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| default:Reihe_C/41/ZNC-1986-41c-0172.pdf | | | | Identifier
| ZNC-1986-41c-0172 | | | | Volume
| 41 | |
| 2 | Author
| G. Ünter Krause, Helmut Simon | Requires cookie* | | | Title
| Design and Applications of Sensitive Enzyme Immunoassays Specific for Clostridial Enoate Reductases | | | | Abstract
| Rabbit antisera raised against purified enoate reductase from Clostridium tyrobutyricum (DSM 1460) and horse-radish peroxidase-conjugated staphylococcal protein A or a/ift-rabbit immuno globulin G, respectively, were used to develop enzyme immunoassays. Sensitivity limits of the assay are about 250 pg antigen if the enzyme immunoassays are performed on membrane filters and examined visually, and 20 pg for tests in aqueous solution with spectrophotometrical evalua tion. The procedures were applied for dot and Western blots as well as colony lifts. Immunologi cal distances between enoate reductases from different Clostridia were determined and the amounts of antigen present in bacterial crude extracts were estimated. In crude extracts of C. thermoaceticum a protein of approximately the size of the enoate reductase and its subunits from C. tyrobutyricum was immunologically detected. Gel filtration chromatography of identically pretreated crude extracts from C. thermoaceticum and C. tyrobuty ricum produced immunological signals at similar molecular weights and revealed a lesser tendency of the presumed thermophilic enoate reductase from C. thermoaceticum to disintegrate into its subunits and fragments as compared to its mesophilic counterpart. | | | |
Reference
| Z. Naturforsch. 44c, 345 (1989); received January 16 1989 | | | |
Published
| 1989 | | | |
Keywords
| Clostridia, Enoate Reductase, Immunoassay, Immunological Distance | | | |
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| default:Reihe_C/44/ZNC-1989-44c-0345.pdf | | | | Identifier
| ZNC-1989-44c-0345 | | | | Volume
| 44 | |
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