The enzymatic synthesis and properties of ribulose 1,5-diphosphate.
نویسندگان
چکیده
These enzymatic reactions have been utilized for t,he preparation of RuDP. In the present paper the isolation procedure and proof of structure of RuDP are described, together with some of the properties of this compound. The availability of substrate quantities of RuDP has permitted a direct study of its reaction with CO2 and the purification of the carboxylation enzyme.2 This work will be reported in a publication t,o follow. With purified preparations from spinach, the reaction
منابع مشابه
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...
متن کاملRibulose 1,5-Diphosphate Carboxylase Synthesis in Euglena: II. Effect of Inhibitors on Enzyme Synthesis during Regreening and Subsequent Transfer to Darkness.
Dark-grown Euglena gracilis Klebs strain Z Pringsheim cells, which have been partially regreened in the light, show a striking, continued synthesis of the chloroplast enzyme ribulose 1,5-diphosphate carboxylase on transfer back into darkness. This dark synthesis of the enzyme was completely prevented by the addition of 15 mug/ml of cycloheximide to the culture medium but was unaffected, for at ...
متن کاملEvidence for in vivo Light-induced Synthesis of Ribulose-1,5-diP Carboxylase and Phosphoribulokinase in Greening Barley Leaves.
WHEN ACTINOMYCIN D, PUROMYCIN, STREPTOMYCIN, CHLORAMPHENICOL, AND CYCLOHEXIMIDE, KNOWN INHIBITORS OF PROTEIN SYNTHESIS, WERE APPLIED TO LEAVES OF INTACT SEEDLINGS OR DETACHED LEAVES OF BARLEY PRIOR TO THEIR GREENING, THE SAME GENERAL RESPONSE RESULTED: the light-induced increase in activity of ribulose 1,5-diphosphate carboxylase was prevented while that of phosphoribulokinase was only partiall...
متن کاملPurification and Some Properties of Chlorella fusca Ribulose 1,5-Diphosphate Carboxylase.
Ribulose 1,5-diphosphate carboxylase has been purified from extracts of autotrophically grown Chlorella fusca by ammonium sulfate precipitation and centrifugation on a linear sucrose density gradient. The enzyme was homogeneous by the criterion of polyacrylamide gel electrophoresis. The molecular weight of the enzyme was 530,000, and it was composed of two types of subunit of molecular weight 5...
متن کاملThe presence of ribulose 1,5-diphosphate carboxylase in the nonphotosynthetic endosperm of germinating castor beans.
Ribulose 1,5-diphosphate carboxylase was detected in extracts of germinating castor bean (Ricinus communis var. Hale) endosperms. This is the first report of this enzyme in a nonphotosynthetic (no chlorophyll) plant tissue. Radioactive 3-phosphoglyceric acid has been identified as the principle product resulting from the enzymatic condensation of (14)C-bicarbonate and ribulose-1,5-diP in endosp...
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ورودعنوان ژورنال:
- The Journal of biological chemistry
دوره 218 2 شماره
صفحات -
تاریخ انتشار 1956