Chlorophyll, Ribulose-1,5-diphosphate Carboxylase, and Hill Reaction Activity in Developing Leaves of Populus deltoides

Chlorophyll, Ribulose-1,5-diphosphate Carboxylase, and Hill Reaction Activity in Developing Leaves of Populus deltoides.

The synthesis of chlorophyll and ribulose diphosphate carboxylase as well as the development of Hill reaction activity were followed in expanding Populus deltoides leaves and related to photosynthetic patterns. Total chlorophyll, which was not correlated with photosynthetic rate in expanding leaves, decreased slightly with age in very young leaves, due to a decrease in chlorophyll b, but then i...

Ribulose Diphosphate Carboxylase / Oxygenase

The stimulation or inhibition of ribulose diphosphate oxygenase by a variety of compounds is compared with the reported effects on these compounds on the ribulose diphosphate carboxylase activity. A possible transition state analog of ribulose diphosphate, Z-carboxyribitol 1 ,5-diphosphate, at a molar ratio of inhibitor to enzyme of 10 to 1, irreversibly inactivates the oxygenase and carboxylas...

Ribulose Diphosphate Carboxylase in Thiorhodaceae.

Evidence for lack of turnover of ribulose 1,5-diphosphate carboxylase in barley leaves.

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...

Light-induced de Novo Synthesis of Ribulose 1,5-Diphosphate Carboxylase in Greening Leaves of Barley.

An antibody specific for ribulose 1,5-diphosphate carboxylase was used to isolate the enzyme from greening barley (Hordeum vulgare L.) leaves. The increase in enzymatic activity during greening was due to de novo synthesis of the enzyme. Increases in enzymatic activity were accompanied by corresponding increases in enzyme protein and by incorporation of radioactive leucine, all of which were in...