NAD+ Kinase Activities in Euglena Gracilis and Phaseolus Vulgaris
| Autor: | Isabelle S Lucet, M.C. Morère-Le Paven, R. Jalouzot, Françoise Montrichard, Danielle L. Laval-Martin |
|---|---|
| Rok vydání: | 1997 |
| Předmět: |
chemistry.chemical_classification
Euglena gracilis biology ved/biology ved/biology.organism_classification_rank.species Dehydrogenase Plant Science Horticulture Reductase Molecular biology Enzyme Glycerol-3-phosphate dehydrogenase chemistry Biochemistry biology.protein NAD+ kinase Kinase activity Alcohol dehydrogenase |
| Zdroj: | Biologia plantarum. 39:565-574 |
| ISSN: | 1573-8264 0006-3134 |
| Popis: | After an electrophoretic separation of proteins from Euglena gracilis and dry seeds of Phaseolus vulgaris in native conditions in polyacrylamide gels, gels were incubated in mixtures containing NAD+, Mg-ATP2-, glucose 6-phosphate, G6P dehydrogenase, and either phenazine ethosulfate and 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyl-tetrazolium bromide (PES/MTT) or phenazine methosulfate and nitro blue tetrazolium (PMS/NBT) as coupled redox system for NAD+ kinase activity detection. In the presence of PES/MTT, 4 bands were revealed for E. gracilis, among which two corresponded to NAD+ kinase activity, the other corresponding to a NAD+ reductase activity due to alcohol dehydrogenase (ADH). In the presence of PMS/NBT, only the bands of NAD+ kinase activity were revealed. With Phaseolus vulgaris, 3 bands of ADH were always revealed in both mixtures, and only the use of PMS/NBT allowed the detection of NAD+ kinase as a fourth band. With both materials, NAD+ reductase staining in gels was intensifed in the presence of GTP or ATP and even further with ADP or GDP. The results demonstrate that: 1) the NAD+ kinase and NAD+ reductase are two distinct enzymes; 2) the NAD+ reductase corresponds to ADH. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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