Evidence for Lack of Turnover of Ribulose 1,5-Diphosphate Carboxylase in Barley Leaves
AUTOR(ES)
Peterson, L. W.
RESUMO
Turnover of ribulose 1,5-diphosphate carboxylase in barley leaves (Hordeum vulgare L.) was followed over time in light and dark. The enzyme was degraded in prolonged darkness and was resynthesized after the plants were returned to light. Labeling with 14C showed that simultaneous synthesis and degradation (turnover) did not occur in light. In contrast, the remaining soluble protein was turned over rapidly in light. Although ribulose 1,5-diP carboxylase can be both degraded and synthesized, these processes seem not to occur simultaneously, but can be induced independently by changing environmental conditions.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=366400Documentos Relacionados
- Light-induced de Novo Synthesis of Ribulose 1,5-Diphosphate Carboxylase in Greening Leaves of Barley
- Loss of Ribulose 1,5-Diphosphate Carboxylase and Increase in Proteolytic Activity during Senescence of Detached Primary Barley Leaves
- A Simplified Purification and Some Properties of Ribulose 1,5-Diphosphate Carboxylase from Barley
- Inhibition of Ribulose 1,5-Diphosphate Carboxylase by 6-Phosphogluconate 1
- Ribulose 1,5-Diphosphate Carboxylase Activity in Relation to Photosynthesis by Intact Leaves And Isolated Chloroplasts. 12