A Thioredoxin-Mediated Activation of Glutamine Synthetase and Glutamate Synthase in Synchronous Chlorella sorokiniana
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منابع مشابه
A Thioredoxin Activated Glutamine Synthetase in Chlorella
Glutam ine synthetase was partly purified from Chlorella pyrenoidosa. This enzyme activity was stimulated by dithioerythritol and 2'-3'-dimercaptopropanol (BAL). Full activation was obtained by thioredoxins isolated from the cyanobacterium Synechococcus 6301, from spinach and by heated Chlorella extract. The apparent Km for the purified thioredoxin B from Synechococcus 6301 was determined to be...
متن کاملCharacterization of glutamine synthetase isoforms from chlorella.
Ion-exchange chromatography of extracts derived from Chlorella sorokiniana mutant strain (oxygen resistant) yielded two separate activity peaks of glutamine synthetase (GS). GS(I) and GS(II) were purified 220- and 187-fold and have molecular weights of approximately 398,000 and 360,000, respectively. Both enzymes are composed of eight identical subunits with a subunit molecular weight of 47,000...
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Exposure of Chlorella sorokiniana (07-11-05) to ozone inhibits photosynthesis. In this study, the effects of ozone on O(2) evolution and fluorescence yields are used to characterize this inhibition. At an ozone dose of about 3 micromoles delivered to 2 x 10(9) cells, the photosynthetic rate of the cells is inhibited 50%, as indicated by a decrease in bicarbonate-stimulated O(2) evolution (contr...
متن کاملGlutamine synthetase-glutamate synthase pathway and glutamate dehydrogenase play distinct roles in the sink-source nitrogen cycle in tobacco.
Glutamate (Glu) metabolism and amino acid translocation were investigated in the young and old leaves of tobacco (Nicotiana tabacum L. cv Xanthi) using [15N]ammonium and [2-15N]Glu tracers. Regardless of leaf age, [15N]ammonium assimilation occurred via glutamine synthetase (GS; EC 6.1.1.3) and Glu synthase (ferredoxin [Fd]-GOGAT; EC 1.4.7.1; NADH-GOGAT; EC 1.4.1.14), both in the light and dark...
متن کاملAmmonium assimilation in Rhizobium phaseoli by the glutamine synthetase-glutamate synthase pathway.
Evidence from in vitro and in vivo studies showed that in Rhizobium phaseoli ammonium is assimilated by the glutamine synthetase (GS)-glutamate synthase NADPH pathway. No glutamate dehydrogenase activity was detected. R. phaseoli has two GS enzymes, as do other rhizobia. The two GS activities are regulated on the basis of the requirement for low (GSI) or high (GSII) ammonium assimilation. When ...
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ژورنال
عنوان ژورنال: Plant Physiology
سال: 1982
ISSN: 0032-0889,1532-2548
DOI: 10.1104/pp.70.1.113