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  • 1
    Electronic Resource
    Electronic Resource
    Crystallization of Helix pomatia agglutinin (HPA), a protein from the edible snail (1999)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 55 (1999), S. 1903-1905 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: Crystals of Helix pomatia agglutinin (HPA) have been grown by the hanging-drop technique using polyethylene glycol as the precipitant at 293 K. Over a period of one to two weeks the crystals grew to maximum dimensions of 0.10 × 0.05 × 0.02 mm. The crystals belong to space group P6322, with unit-cell dimensions a = b = 63.3, c = 105.2 Å and Z = 12 identical monomers of Mr = 13 kDa, aggregating into two 78 kDa hexameric protein molecules per unit cell, each with symmetry 32 (D3). The diffraction pattern extends to 3.6 Å at 293 K.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444999007957
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  • 2
    Electronic Resource
    Electronic Resource
    Crystallization of Helix pomatia agglutinin (HPA), a protein from the edible snail. Erratum (2000)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 56 (2000), S. 109-109 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: One of the authors was omitted in the published version of the paper by Lisgarten et al. (1999) Acta Cryst. D55, 1903–1905. The full author list is given above.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444999015814
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Immobilized enzymes as tools for the demonstration of metabolon formation. A short overview (1993)
    Chicester [u.a.] : Wiley-Blackwell
    Journal of Molecular Recognition 6 (1993), S. 195-204 
    Details
    ISSN: 0952-3499
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: In recent years it has become clear that a cell cannot be visualized as a ‘bag’ filled with enzymes dissolved in bulk water. The aqueous-phase properties in the interior of a cell are, indeed, essentially different from those of an ordianry queous solutin. Large amounts of water are believed to be organized in layers at the surface of intracellular structural proteins and membranes. Such considerations prompt us to reconsider the operation and regulation of metabolic pathways. Enzymes of metabolic pathways are nowadays thought to be clustered and operate as ‘metabolons’. Very often interactions between enzymes of a pathway can exclusively be evidenced in Vitro in media which are known to reduce the water concentration in the vicinity of the proteins. Immobilized enzyme preparations have been shown to be excellent tools for this type of research. We describe here some recent studies where immobilized enzymes have been used in various applications to investigate associations among enzymes of a number of different metabolic pathways (glucolysis/gluconeogenesis, citric acid cycle and its connection to the electron transport chain, aspartate-malate shuttle, glyoxylate cycle). Advantages and disadvantages of the different techniques we also discussed.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jmr.300060408
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  • 4
    Electronic Resource
    Electronic Resource
    Clustering of sequential enzymes in the glycolytic pathway and the citric acid cycle (1990)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 43 (1990), S. 297-306 
    Details
    ISSN: 0730-2312
    Keywords: multienzyme cluster ; complex ; affinity electrophoresis ; metabolic regulation ; channeling ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: In recent years, evidence has been accumulating that metabolic pathways are organized in vivo as multienzyme clusters. Affinity electrophoresis proves to be an attractive in vitro method to further evidence specific associations between purified consecutive enzymes from the glycolytic Pathway on the one hand, and from the citric acid cycle on the other hand. Our results support the hypothesis of cluster formation between the glycolytic enzymes aldolase, glyceraldehydephosphate dehy-drogenase, and triosephosphate isomerase, and between the cycle enzymes fumarase, malate dehydrogenase, and citrate synthase. A model is presented to explain the possibility of regulation of the citric acid cycle by varying enzyme-enzyme associations between the latter three enzymes, in response to changing local intramitochondrial ATP/ADP ratios.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcb.240430402
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    Paper (German National Licenses)
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