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Cell Cycle-related and Endogenously Controlled Circadian Photosynthetic Rhythms in Euglena.
Plant Physiol
March 1979
Division of Biological Sciences, State University of New York, Stony Brook, New York 11794.
The data presented for three strains of Euglena gracilis corroborate previous reports of a diel rhythm in photosynthetic capacity in division-synchronized cultures of this alga and extend these studies to free running, dividing and nondividing (stationary) cultures maintained in either 24-hour or 40-minute cycles of light and darkness. During synchronous growth entrained by LD: 12,12 or free running under LD: 1/3,1/3, photosynthetic CO(2) fixation was rhythmic with a period (24.0 or about 30 hours) corresponding to the period of the cell division rhythm in the population.
View Article and Find Full Text PDFThe glycolate pathway and photosynthetic competence in euglena.
Plant Physiol
January 1975
Postgraduate School of Studies in Biological Sciences, University of Bradford, Bradford, Yorkshire BD7 1DP, England.
The development of glycolate pathway enzymes has been determined in relation to photosynthetic competence during the regreening of Euglena cultures. Phosphoglycolate phosphatase and glycolate dehydrogenase rapidly reached maximal levels of activity but the complete development of ribulose 1,5-diphosphate carboxylase and concomitant photosynthetic carbon dioxide fixation were not attained until 72 hours of illumination. Specific inhibitors of protein synthesis showed that the formation of ribulose 1,5-diphosphate carboxylase in both division-synchronized and regreening cultures was prevented by both cycloheximide and d-threo-chloramphenicol, whereas phosphoglycolate phosphatase formation was only inhibited by d-threo-chloramphenicol but not by l-threo-chloramphenicol or cycloheximide.
View Article and Find Full Text PDFThe Effect of Light on the Synthesis of Mitochondrial Enzymes in Division-synchronized Euglena Cultures.
Plant Physiol
April 1974
Postgraduate School of Studies in Biological Sciences, University of Bradford, Bradford, Yorkshire BD7 1DP, England.
The development of the mitochondrial enzymes fumarase and succinate dehydrogenase has been followed in Euglena cultures division-synchronized by 14-hour light periods alternating with 12-hour dark periods. The activity of both enzymes was unaltered over the light phase, doubled in early dark phase, and thereafter remained constant over the rest of the cycle. The increase in enzyme activity in early dark phase probably represented de novo enzyme synthesis because it was prevented by the addition of cycloheximide at a concentration known to inhibit protein synthesis on Euglena cytoplasmic ribosomes.
View Article and Find Full Text PDFMalate dehydrogenase isoenzymes in division synchronized cultures of euglena.
Plant Physiol
June 1973
Postgraduate School of Studies in Biological Sciences, University of Bradford, Bradford, Yorkshire BD7 1DP, England.
Sucrose density gradient centrifugation of broken cell suspensions of autotrophically grown Euglena gracilis Klebs. has allowed the separation of chloroplasts, mitochondria, and peroxisomes. Chlorophyll was taken as a marker for chloroplasts, fumarase and succinate dehydrogenase for mitochondria, and glycolate oxidoreductase for peroxisomes.
View Article and Find Full Text PDFThe regulation of glycolate metabolism in division synchronized cultures of euglena.
Plant Physiol
May 1971
Postgraduate School of Studies in Biological Sciences, University of Bradford, Bradford BD7 1DP, Yorkshire, England.
Phosphoglycolate and phosphoglycerate phosphatases and glycolate dehydrogenase activities were determined in division synchronized Euglena gracilis strain Z cultures. Phosphoglycolate phosphatase activity remained nearly constant in the light but doubled in the dark, whereas phosphoglycerate phosphatase activity decreased by half in the light and increased 4-fold over the dark phase of the cycle. Glycolate dehydrogenase activity assayed by dye reduction increased over the light and remained constant during the dark phase, but when determined by the phenylhydrazone method, an assay dependent upon the presence of a natural hydrogen acceptor, activity decreased in the dark phase.
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