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. 1973 Jun;51(6):1042–1045. doi: 10.1104/pp.51.6.1042

Evidence for Lack of Turnover of Ribulose 1,5-Diphosphate Carboxylase in Barley Leaves

L W Peterson 1, G E Kleinkopf 1, R C Huffaker 1
PMCID: PMC366400  PMID: 16658461

Abstract

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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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