Department of Agronomy and Range Science, University of California, Davis, California 95616.
Plant Physiol. 1973 Jun;51(6):1042-5. doi: 10.1104/pp.51.6.1042.
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 (14)C 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.
在光暗条件下追踪大麦叶片（Hordeum vulgare L.）中核酮糖 1,5-二磷酸羧化酶的周转率。该酶在长时间的黑暗中降解，并在植物返回光照后重新合成。用（14）C 标记表明，在光照下同时发生合成和降解（周转）不会发生。相比之下，剩余的可溶性蛋白在光照下迅速周转。尽管核酮糖 1,5-二磷酸羧化酶可以降解和合成，但这些过程似乎不会同时发生，而是可以通过改变环境条件独立诱导。
