Results 111 to 120 of about 20,337 (159)
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Thiamin uptake in Euglena gracilis
Biochimica et Biophysica Acta (BBA) - Molecular Cell Research, 1987Thiamin uptake has been investigated in Euglena gracilis Z. This protozoon possessed an active transport system for thiamin with a Km value of 17 nM and a Vmax value of 7.8 pmol per 10(6) cells per min. Thiamin uptake was dependent on pH and temperature, but not on exogenous glucose as an energy source.
S, Shigeoka +4 more
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Ferredoxin biosynthesis in Euglena gracilis
Biochimica et Biophysica Acta (BBA) - Nucleic Acids and Protein Synthesis, 1976Analysis of ferredoxin content in cultures of Euglena gracilis grown in the presence of selective antibiotic inhibitors of protein synthesis resulted in the following conclusions: 1. Ferredoxin is synthesized from cytoplasmic (80s-type) ribosomes; cycloheximide, a potent inhibitor of 80s translation completely abolished the synthesis, while the ...
R S, Matson, T, Kimura
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Mitomycins and the bleaching of Euglena gracilis
Archiv für Mikrobiologie, 1969The effects of some mitomycin antibiotics on the chloroplast system of Euglena gracilis were studied. Only those derivatives which contained an alkyl group on the aziridine nitrogen were effective bleaching agents. Thus, only N-methyl-mitomycin, porfiromycin, and mitomycin B caused a highly significant loss of chloroplasts.
L, Ebringer, J L, Mego, A, Jurásek
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Heteroxanthin in Euglena gracilis
Archiv f�r Mikrobiologie, 19731. From a large scale preparation of Euglena gracilis, strain Z, besides the acetylenic pigments diatoxanthin and diadinoxanthin and the allene neoxanthin, an additional acetylenic xanthophyll has been isolated. 2. Mass and IR spectra and chemical reactions showed typical patterns of heteroxanthin from Vaucheria. 3.
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Versatile biotechnological applications of Euglena gracilis
World Journal of Microbiology and Biotechnology, 2023Euglena gracilis is a freshwater protist possessing secondary chloroplasts of green algal origin. Various physical factors (e.g. UV) and chemical compounds (e.g. antibiotics) cause the bleaching of E. gracilis cells-the loss of plastid genes leading to the permanent inability to photosynthesize. Bleaching can be prevented by antimutagens (i.e.
Diana Lihanová +6 more
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Gravitaxis and graviperception in euglena gracilis
Advances in Space Research, 1998Gravitactic orientation in the flagellate Euglena gracilis is mediated by an active physiological receptor rather than a passive alignment of the cells. During a recent space flight on the American shuttle Columbia the cells were subjected to different accelerations between 0 and 1.5 x g and tracked by computerized real-time image analysis.
D P, Hader, M, Lebert, P, Richter
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Euglena gracilis cytochrome 558
Biochimica et Biophysica Acta (BBA) - Bioenergetics, 1972Abstract Euglena gracilis contains both the classical cytochrome f (cytochrome c 552 ) found in algae and plants, and an atypical cytochrome 558, which has covalently bound heme. We report here some of the chemical and physical properties of cytochrome 558, including amino acid composition, molecular size, and spectral properties.
T E, Meyer, M A, Cusanovich
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Biosynthesis of Phosphatidylcholine in Euglena gracilis*†
The Journal of Protozoology, 1966SYNOPSIS. Extracts of Euglena gracilis carry out a very rapid but limited synthesis of phosphatidylcholine when S‐adenosylmethionine or ATP and methionine are supplied. Cytidinediphosphocholine apparently is not utilized. Qualitatively the same results are obtained whether the cells are light‐ or dark‐grown.
C L, Tipton, M D, Swords
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Respiratory cytochromes of Euglena gracilis
Biochimica et Biophysica Acta (BBA) - Bioenergetics, 1969Abstract 1. 1. Difference spectra of whole cells and of a particulate fraction of a streptomycin-bleached strain of Euglena gracilis showed the presence of a b -type cytochrome, cytochrome b (561 Euglena), and an a -type cytochrome, cytochrome a -type (609 Euglena). The cytochromes were characterized by pyridine hemochromogen formation and
J K, Raison, R M, Smillie
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Functional Conservation of Calreticulin in Euglena gracilis
Journal of Eukaryotic Microbiology, 1998Calreticulin is the major high capacity, low affinity Ca2+ binding protein localized within the endoplasmic reticulum. It functions as a reservoir for triggered release of Ca2+ by the endoplasmic reticulum and is thus integral to eukaryotic signal transduction pathways involving Ca2+ as a second messenger.
NAVAZIO, LORELLA +9 more
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