| Literature DB >> 16666925 |
S J Tchuinmogne1, C Huault, A Aoues, A P Balangé.
Abstract
We have compared the activity of 5-aminolevulinate dehydratase (5-ALAD) with the amount of protein detected by specific antibodies in rocket immunoelectrophoresis. Parallel kinetic evolutions of enzymic activity and amount of antigen were observed in radish (Raphanus sativus L.) cotyledons, both in complete darkness or under standard far red light involving phytochrome. However, the treatment of seedlings with gabaculine leads to an important decrease in enzymic activity, while the specific protein content is maintained. This inhibition is not overcome by the addition of glutamic acid, but by 5-aminolevulinic acid which points to a specific control of 5-ALAD activity by its substrate. As there is no discrepancy between the enzymic activity and the amount of antigen during the time course development of seedlings, this could confirm a coordinate cellular control between 5-aminolevulinic acid formation and 5-ALAD protein synthesis, both being amplified by the action of phytochrome.Entities:
Year: 1989 PMID: 16666925 PMCID: PMC1061885 DOI: 10.1104/pp.90.4.1293
Source DB: PubMed Journal: Plant Physiol ISSN: 0032-0889 Impact factor: 8.340