Isolation and identification of cytokinins from Euglena gracilis transfer ribonucleic acid

Biochemistry ◽  
1977 ◽  
Vol 16 (7) ◽  
pp. 1355-1360 ◽  
Author(s):  
Santhanam Swaminathan ◽  
Robert M. Bock
Keyword(s):  
Euglena Gracilis ◽  
Ribonucleic Acid ◽  
Isolation And Identification

Messenger ribonucleic acid function and protein synthesis in zinc-deficient Euglena gracilis

Biochemistry ◽  
1982 ◽  
Vol 21 (21) ◽  
pp. 5359-5363 ◽  
Author(s):  
L. Gail Crossley ◽  
Kenneth H. Falchuk ◽  
Bert L. Vallee
Keyword(s):  
Protein Synthesis ◽  
Euglena Gracilis ◽  
Ribonucleic Acid ◽  
Messenger Ribonucleic Acid ◽  
Acid Function

Isolation and identification of four cytokinins from wheat germ transfer ribonucleic acid

Biochemistry ◽  
1970 ◽  
Vol 9 (9) ◽  
pp. 1867-1872 ◽  
Author(s):  
W. John Burrows ◽  
Donald J. Armstrong ◽  
M. Kaminek ◽  
Folke Skoog ◽  
Robert M. Bock ◽  
...  
Keyword(s):  
Ribonucleic Acid ◽  
Wheat Germ ◽  
Isolation And Identification

Organization of the Pellicle and the Muciferous Glands in Euglena Gracilis

1970 ◽  
Vol 28 ◽  
pp. 104-105
Author(s):  
Hilton H. Mollenhauer ◽  
W. Evans
Keyword(s):  
Plasma Membrane ◽  
Euglena Gracilis ◽  
Complex Forms ◽  
Secondary Periodicity

The pellicular structure of Euglena gracilis consists of a series of relatively rigid strips (Fig. 1) composed of ridges and grooves which are helically oriented along the cell and which fuse together into a common junction at either end of the cell. The strips are predominantly protein and consist in part of a series of fibers about 50 Å in diameter spaced about 85 Å apart and with a secondary periodicity of about 450 Å. Microtubules are also present below each strip (Fig. 1) and are often considered as part of the pellicular complex. In addition, there may be another fibrous component near the base of the pellicle which has not yet been very well defined.The pellicular complex lies underneath the plasma membrane and entirely within the cell (Fig. 1). Each strip of the complex forms an overlapping junction with the adjacent strip along one side of each groove (Fig. 1), in such a way that a certain amount of sideways movement is possible between one strip and the next.

Immunocytochemical studies on the behavior of RuBisCO and LHCP II during the cell cycle of synchronized Euglena gracilis

1990 ◽  
Vol 48 (3) ◽  
pp. 662-663
Author(s):  
Tetsuaki Osafune ◽  
Shuji Sumida ◽  
Tomoko Ehara ◽  
Eiji Hase ◽  
Jerome A. Schiff
Keyword(s):  
Cell Cycle ◽  
Immunoelectron Microscopy ◽  
Growth Phase ◽  
Euglena Gracilis ◽  
Dark Period ◽  
Light Period ◽  
Carboxylase Activity ◽  
Immunocytochemical Studies ◽  
Lhcp Ii

Changes in the morphology of pyrenoid and the distribution of RuBisCO in the chloroplast of Euglena gracilis were followed by immunoelectron microscopy during the cell cycle in a light (14 h)- dark (10 h) synchronized culture under photoautotrophic conditions. The imrnunoreactive proteins wereconcentrated in the pyrenoid, and less densely distributed in the stroma during the light period (growth phase, Fig. 1-2), but the pyrenoid disappeared during the dark period (division phase), and RuBisCO was dispersed throughout the stroma. Toward the end of the division phase, the pyrenoid began to form in the center of the stroma, and RuBisCO is again concentrated in that pyrenoid region. From a comparison of photosynthetic CO2-fixation with the total carboxylase activity of RuBisCO extracted from Euglena cells in the growth phase, it is suggested that the carboxylase in the pyrenoid functions in CO2-fixation in photosynthesis.

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