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  • 1
    ISSN: 1520-4804
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    [s.l.] : Nature Publishing Group
    Nature 385 (1997), S. 275-278 
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] PGK is a monomeric enzyme composed of N- and C-terminal domains connected by a well-conserved hinge region. In all previously reported crystal structures, bound substrates are too far apart to permit catalysis. This has been explained both by a hinge-bending mechanism that can approximate the ...
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  • 3
    Electronic Resource
    Electronic Resource
    Springer
    Journal of molecular evolution 24 (1986), S. 45-52 
    ISSN: 1432-1432
    Keywords: Trypanosome ; Glycosome ; Gene ; Housekeeping proteins ; VSGs ; Phylogeny ; Codon usage ; Telomere
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The genes for four glycolytic enzymes ofTrypanosoma brucei have been analyzed. The proteins encoded by these genes show 38–57% identity with their counterparts in other organisms, whether pro- or eukaryotic. These data are consistent with a phylogenetic tree in which trypanosomes diverged very early from the main branch of the eukaryotic lineage. No definite conclusion can be drawn yet about the evolutionary origin of glycosomes, the microbodies of trypanosomes which contain most enzymes of the glycolytic pathway. A bias could be observed in the codon usage of the glycolytic genes and genes for other housekeeping proteins, indicating that trypanosomes may have selected a nucleotide sequence that enables efficient translation. However, the genes for variant surface glycoproteins (VSGs) do not show such a bias. This lack of preference for special codons is explained by the high evolutionary rate that could be observed for VSG genes.
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  • 4
    ISSN: 1432-1432
    Keywords: Trypanoplasma borelli ; Kinetoplastida ; Glyceraldehyde-3-phosphate dehydrogenase ; Glycosome ; Compartmentation ; Isoenzymes
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract In Trypanoplasma borelli, a representative of the Bodonina within the Kinetoplastida, glyceraldehyde-3-phosphate dehydrogenase (GAPDH) activity was detected in both the cytosol and glycosomes. This situation is similar to that previously found in Trypanosomatidae, belonging to a different Kinetoplastida suborder. In Trypanosomatidae different isoenzymes, only distantly related, are responsible for the activity in the two cell compartments. In contrast, immunoblot analysis indicated that the GAPDH activity in cytosol and glycosomes of T. borelli should be attributed to identical or at least very similar proteins related to the glycosomal GAPDH of Trypanosomatidae. Moreover, only genes related to the glycosomal GAPDH genes of Trypanosomatidae could be detected. All attempts to identify a gene related to the one coding for the trypanosomatid cytosolic GAPDH remained unsuccessful. Two tandemly arranged genes were found which are 95% identical. The two encoded polypeptides differ in 17 residues. Their sequences are 72–77% identical to the glycosomal GAPDH of the other Kinetoplastida and share with them some characteristic features: an excess of positively charged residues, specific insertions, and a small carboxy-terminal extension containing the sequence -AKL. This tripeptide conforms to the consensus signal for targeting of proteins to glycosomes. One of the two gene copies has undergone some mutations at positions coding for highly conserved residues of the active site and the NAD+-binding domain of GAPDH. Modeling of the protein's three-dimensional structure suggested that several of the substitutions compensate each other, retaining the functional coenzyme-binding capacity, although this binding may be less tight. The presented analysis of GAPDH in T. borelli gives further support to the assertion that one isoenzyme, the cytosolic one, was acquired by horizontal gene transfer during the evolution of the Kinetoplastida, in the lineage leading to the suborder Trypanosomatina (Trypanosome, Leishmania), after the divergence from the Bodonina (Trypanoplasma). Furthermore, the data clearly suggest that the original GAPDH of the Kinetoplastida has been compartmentalized during evolution.
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  • 5
    Electronic Resource
    Electronic Resource
    [s.l.] : Nature Publishing Group
    Nature 303 (1983), S. 592-597 
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Some of the genes for the variant surface glycoproteins of trypanosomes are located close to a discontinuity in the DNA, presumably a chromosome end. We show here that DNA fragments containing these telomeres increase in length in multiplying trypanosomes at a rate of about 10 base pairs per ...
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  • 6
    ISSN: 1432-072X
    Keywords: Rhodopseudomonas sphaeroides ; Proton motive force ; Ion-permeability ; Chromatophores
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The magnitude and composition of the proton motive force $$(\Delta \tilde \mu _{{\rm H}^ + } )$$ has been measured in chromatophores and whole cells of Rhodopseudomonas sphaeroides as a function of the ionic composition of the buffer in which the energy-transducing membranes are suspended. Measurements with the flow-dialysis technique are compared with spectrophotometric measurements of the absorbance changes of carotenoids and of the quenching of the fluorescence of 9-aminoacridine. It is concluded that the optical techniques give rise to an overestimation of the gradients of pH and electrical potential. However, with the optical techniques the relative permeability of the membrane of R. sphaeroides for various cations and anions can be estimated. The results indicate that in general anions are more permeant than cations; the relative permeability of the anions is: $$SO_4^ = 〈 HPO_4^ = 〈 Cl^ - 〈 NO_3^ - 〈 ClO_4^ -$$ .
    Type of Medium: Electronic Resource
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  • 7
    Electronic Resource
    Electronic Resource
    Springer
    Journal of bioenergetics and biomembranes 27 (1995), S. 513-525 
    ISSN: 1573-6881
    Keywords: Trypanosoma brucei ; glycolysis ; glycosome ; flux control ; Metabolic Control Analysis ; diffusion
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Physics
    Notes: Abstract Unlike other eukaryotic cells, trypanosomes possess a compartmentalized glycolytic pathway. The conversion of glucose into 3-phosphoglycerate takes place in specialized peroxisomes, called glycosomes. Further conversion of this intermediate into pyruvate occurs in the cytosol. Due to this compartmentation, many regulatory mechanisms operating in other cell types cannot work in trypanosomes. This is reflected by the insensitivity of the glycosomal enzymes to compounds that act as activity regulators in other cell types. Several speculations have been raised about the function of compartmentation of glycolysis in trypanosomes. We calculate that even in a noncompartmentalized trypanosome the flux through glycolysis should not be limited by diffusion. Therefore, the sequestration of glycolytic enzymes in an organelle may not serve to overcome a diffusion limitation. We also search the available data for a possible relation between compartmentation and the distribution of control of the glycolytic flux among the glycolytic enzymes. Under physiological conditions, the rate of glycolytic ATP production in the bloodstream form of the parasite is possibly controlled by the oxygen tension, but not by the glucose concentration. Within the framework of Metabolic Control Analysis, we discuss evidence that glucose transport, although it does not qualify as the sole rate-limiting step, does have a high flux control coefficient. This, however, does not distinguish trypanosomes from other eukaryotic cell types without glycosomes.
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  • 8
    Electronic Resource
    Electronic Resource
    Springer
    Journal of bioenergetics and biomembranes 26 (1994), S. 205-212 
    ISSN: 1573-6881
    Keywords: Glycosome ; microbody ; glycalysis ; biogenesis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Physics
    Notes: Abstract Glycosomes are intracellular, microbody-like organelles found in all members of the protist order Kinetoplastida examined. Nine enzymes involved in glucose and glycerol metabolism are associated with these organelles. These enzymes are involved in pathways which, in other organisms, are usually located in the cytosol. This paper reviews our current knowledge about the glycosome and its constituent enzymes, with special reference to the organelle ofTrypanosoma brucei.
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  • 9
    Electronic Resource
    Electronic Resource
    Springer
    Journal of bioenergetics and biomembranes 26 (1994), S. 213-219 
    ISSN: 1573-6881
    Keywords: Glycosome ; microbody ; glycolysis ; evolution
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Physics
    Notes: Abstract The available data on carbohydrate metabolism in Kinetoplastida have been reviewed. Based on the metabolic pattern of different kinetoplastid organisms, on the subcellular distribution of their glycolytic enzymes, and on the structural and regulatory properties of these proteins, we propose that the glycosome developed from an endosymbiont, as a specific manner to control carbohydrate and energy metabolism. It is discussed how the enzymes were subcellularly recompartmentalized during evolution as adaptation to the environment encountered by the organisms.
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  • 10
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