Isoenzymes of sugar phosphate metabolism in endosperm of germinating castor beans.

نویسندگان

  • M Nishimura
  • H Beevers
چکیده

Two isoenzymes each of phosphoglucomutase, hexose phosphate isomerase, aldolase, fructose diphosphatase, phosphofructokinase, and 6-phosphogluconate dehydrogenase have been separated by DEAE-cellulose column chromatography of extracts from endosperm of germinating castor beans (Ricinus communis cv. Hale). One of each of the enzymes is localized in the cytosol and the other is confined to plastids. Developmental studies of these isoenzymes were carried out to clarify their roles in the endosperm. In extracts from ungerminated seeds the activities of marker enzymes of mitochondria (fumarase), plastids (ribulose bisphosphate carboxylase), and glyoxysomes (catalase) were low, but phosphoglucomutase, hexose phosphate isomerase, aldolase, and 6-phosphogluconate dehydrogenase were present in relatively high activity. The total amounts of these enzymes increased 3- to 4-fold during the first 5 days of growth. The activities of isoenzymes in the plastids rose in parallel with that of ribulose bisphosphate carboxylase to reach a maximum at day 4, and like the carboxylase they declined sharply thereafter. The activities of the cytosolic isoenzymes peaked at day 5. These changes are consistent with the roles previously proposed for the sequences present in plastid and cytosol.

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The 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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Two isoenzymes each of hexose-P isomerase, aldolase and 6-P-gluconate dehydrogenase have been found in the endosperm of developing castor beans (Ricinus communis L.). One isoenzyme for each activity is present in the proplastid fraction. Only one form of glucose-6-P dehydrogenase was found. It is suggested that the partition of an enzyme activity between cytosol and plastid is regulated by the ...

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The breakdown of lipid reserves in the endosperm of germinating castor beans.

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Localization and properties of ribulose diphosphate carboxylase from castor bean endosperm.

A substantial portion of the ribulose 1,5-diphosphate carboxylase activity in the endosperm of germinating castor beans (Ricinus communis var. Hale) is recovered in the proplastid fraction. The partially purified enzyme shows homology with the enzyme from spinach (Spinacia oleracea) leaves, as evidenced by its reaction against antibodies to the native spinach enzyme and to its catalytic subunit...

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Development of ribulose 1,5-diphosphate carboxylase in nonphotosynthetic endosperms of germinating castor beans.

Ribulose 1,5-diphosphate (RuDP) carboxylase has been partially purified from dark-grown nonphotosynthetic endosperms of germinating castor beans (Ricinus communis var. Hale). The Km values for RuDP, HCO(3) (-), and Mg(2+) are 0.51, 33, and 1.78 mm, respectively. The pH optimum for the carboxylation reaction is pH 7.5. Germination is required for the development of the carboxylase in the endospe...

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عنوان ژورنال:
  • Plant physiology

دوره 67 6  شماره 

صفحات  -

تاریخ انتشار 1981