PLASTID DEVELOPMENT IN PRIMARY LEAVES OF PHASEOLUS VULGARIS. VIII. THE EFFECTS OF THE TRANSFER OF DARK-GROWN PLANTS TO CONTINUOUS ILLUMINATION

The development of increased activities of ribulosediphosphate carboxylase (EC 4.1.1.39) and of phosphoribulokinase (EC 2.7.1.19) in greening bean leaves was completely inhibited by D-threo chloramphenicol but unaffected by L-threo chloramphenicol. This indicates that these enzymes are synthesized by the ribosomes of the developing plastids. A different mechanism appears to be responsible for the development of activity of NADP-dependent triosephosphate dehydrogenase (EC 1.2.1.13) where the D-threo isomer gave 45% inhibition and the L-threo isomer gave 18% inhibition. Thus both specific (D-threo isomer) and unspecific (both isomers) inhibition occurred. It is suggested that the development of NADP-dependent triosephosphate dehydrogenase activity may result from the allosteric activation, in the plastids, of the NAD-dependent enzyme (Muller et al., 1969) which has been synthesized by cytoplasmic ribosomes. Neither isomer inhibited the development of five other enzymes of the photosynthetic carbon cycle namely ribosephosphate isomerase (EC 5.3.1.6), phosphoglycerate kinase (EC 2.7.2.3), triosephosphate isomerase (EC 5.3.1.1), tructosediphosphate aldolase (EC 4.1.2.13) and transketolase (EC 2.2.1.1), but there was a significant stimulation of the activity of transketolase by D-threo chloramphenicol.