The Formation of Ribulose Diphosphate Carboxylase Protein during Chloroplast Development in Barley.
نویسنده
چکیده
Ribulose 1,5-diphosphate carboxylase is synthesized in barley leaves growing in the dark. Upon illumination there is a marked increase in the rate of synthesis of the enzyme. The specific activity of the enzyme expressed as cpm incorporated into phosphoglyceric acid per mug of fraction I protein, after isolation shows no change either during dark growth or greening. During early stages of illumination of 7 day dark grown leaves with 320 foot-candles the enzymic activity in the water soluble protein fraction of the leaf shows a short term decline after 15 min which lasts for 30 min. Leaves greening at 2 foot-candles show a similar decline which is shifted to a time between the fourth and eighth hr after the onset of illumination.
منابع مشابه
Loss of Ribulose 1,5-Diphosphate Carboxylase and Increase in Proteolytic Activity during Senescence of Detached Primary Barley Leaves.
Symptoms typical of senescence occurred in green detached primary barley (Hordeum vulgare L.) leaves placed in darkness and in light. Chlorophyll, total soluble protein, ribulose 1,5-diphosphate carboxylase protein and activity each progressively decreased in darkness and to a lesser extent in light. In all treatments most of the total soluble protein lost was accounted for by a decrease in rib...
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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...
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Etioplasts of 4.5-day-old dark-grown barley synthesize and accumulate most of the membrane and nearly all the soluble polypeptides of mature chloroplasts of light-grown seedlings. Etioplasts do not synthesize a limited set of chloroplast-encoded polypeptides which are major constituents of chloroplast thylakoid membranes: two chlorophyll apoproteins of photosystem I (68 and 65 kDa), two chlorop...
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ورودعنوان ژورنال:
- Plant physiology
دوره 44 11 شماره
صفحات -
تاریخ انتشار 1969