Results 171 to 180 of about 5,083 (214)
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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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Laminarase of Euglena gracilis
Science, 1960An enzyme in extracts of the protistan Euglena gracilis splits the polysaccharide laminarin (β-1:3-glucosan). Its optimal p H is 5.0, and it is activated by Mn ++ ions.
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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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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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Identification of a rhodopsin photoreceptor in Euglena gracilis
Biochimica et Biophysica Acta (BBA) - General Subjects, 1992Visual pigments are a class of receptor proteins that absorb light and trigger sensory signals. Retinal-containing proteins are used in nature as photoreceptors mainly in animals vision. Mammalian rhodopsin is the best studied example of a light sensor which couples photon absorption to a cascade of biochemical reactions amplifying the input signal.
GUALTIERI P +3 more
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Ultrastructure of the pellicle ofEuglena gracilis
Tissue and Cell, 2000Deep-etching technique was used to investigate the organization of the pellicle complex of Euglena gracilis. The interpretation of the images was further supported by SEM and TEM investigations. Our results mainly validate data obtained by previous freeze-fracture studies on the E and P faces of the outer cortical membrane.
Vismara, R. +6 more
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Euglena gracilis Subcellular Fractionation
Subcellular fractionation of Euglena gracilis has been conducted for over 50 years in various forms by numerous research groups. The development of this technique is closely tied to the specific organelle or fraction required for specific purposes.Lucia, Tomečková +2 more
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Chelatins in euglena gracilis and ochromonas danica
Comparative Biochemistry and Physiology Part C: Comparative Pharmacology, 1985Amino acid analysis was performed on low molecular weight copper binding proteins purified from two species of Protozoa after exposure to a high level of this metal. The compound from Ochromonas is similar to Cu-chelatins. The two peptides from Euglena have a different molecular weight and a very dissimilar amino acid composition. Peptide No.
Piccinni E. +2 more
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