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  • 1
    Electronic Resource
    Electronic Resource
    Structure and function of chloroplast proteins. XXIV. Spinach leaf ribulosebisphosphate carboxylase. Carboxylase and oxygenase reaction examined by immunochemical methods (1974)
    s.l. : American Chemical Society
    Biochemistry 13 (1974), S. 2277-2281 
    Details
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/bi00708a006
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  • 2
    Electronic Resource
    Electronic Resource
    Purification and characterization of aconitase isoforms from etiolated pumpkin cotyledons (1993)
    Oxford, UK : Blackwell Publishing Ltd
    Physiologia plantarum 88 (1993), S. 0 
    Details
    ISSN: 1399-3054
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Although aconitase (EC 4.2.1.3) is involved in the glyoxylate cycle, which is localized in glyoxysomes, we detected very low aconitase activity in glyoxysomal fractions after sucrose gradient centrifugation of extracts prepared from etiolated pumpkin (Cucurbita sp.) colyledons. Two aconitase isoforms were purified to homogeneity, albeit in low yield, by hydrophobic interaction, hydroxylapatite and anion exchange chromatography. They were designated Aco I and Aco II; both were shown to be monomeric proteins of M1 100 000 or 98 000 by gel filtration and SDS-PAGE analysis, respectively; isoelectric points were 5.0 and 4.8, respectively. Kinetic studies revealed similarities between Aco I and Aco II. A third aconitase isoform (Aco III) was revealed but not purified to homogeneity.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1399-3054.1993.tb01363.x
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  • 3
    Electronic Resource
    Electronic Resource
    Studies on the phase transition in the single lamellar liposomes. 3. Kinetic behavior of the phase transition (1981)
    s.l. : American Chemical Society
    The @journal of physical chemistry 〈Washington, DC〉 85 (1981), S. 1401-1405 
    Details
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology , Physics
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/j150610a026
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  • 4
    Electronic Resource
    Electronic Resource
    Presence of Glyoxylate Cycle Enzymes in the Mitochondria of Euglena gracilis (2003)
    Oxford, UK : Blackwell Publishing Ltd
    The @journal of eukaryotic microbiology 50 (2003), S. 0 
    Details
    ISSN: 1550-7408
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: . Isocitrate lyase and malate synthase are specific enzymes of the glyoxylate cycle, used here as glyoxysomal markers. Both enzymes were found in the mitochondrial fraction after organelle fractionation by isopycnic centrifugation. Electron microscopy of this fraction indicated that mitochondria were the only recognizable organelles. Using an immunogold labeling method with anti-(malate synthase) antiserum, the only organelles stained in cells were the mitochondria. These results show that the glyoxylate cycle is present in mitochondria in Euglena.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1550-7408.2003.tb00239.x
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  • 5
    Electronic Resource
    Electronic Resource
    Purification and characterization of pumpkin long-chain acyl-CoA oxidase (1999)
    Copenhagen : Munksgaard International Publishers
    Physiologia plantarum 106 (1999), S. 0 
    Details
    ISSN: 1399-3054
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Pumpkin (Cucurbita sp.) long-chain acyl-CoA oxidase (ACOX) (EC 1.3.3.6) was purified to homogeneity by hydrophobic interaction, hydroxyapatite, affinity, and anion exchange chromatographies. The purified isoenzyme is a dimeric protein, consisting of two apparently identical 72-kDa subunits. The protein is exclusively localized in glyoxysomes. The enzyme catalyzes selectively the oxidation of CoA esters of fatty acids with 12–18 C atoms and exhibits highest activity with C-14 fatty acids, but no activity with isobutyryl-CoA and isovaleryl-CoA (branched chain) or glutaryl-CoA (dicarboxylic). The enzyme is strongly inhibited by high concentrations of palmitoyl-CoA and weakly inhibited by high concentration of myristoyl-CoA. It is also inhibited by Triton X-100 at concentrations above 0.018% (w/v) the critical micellar concentration. The consequences of the substrate inhibition for the evaluation of long-chain ACOX activity in plant tissues are discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1034/j.1399-3054.1999.106204.x
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  • 6
    Electronic Resource
    Electronic Resource
    A VPE family supporting various vacuolar functions in plants (2005)
    Oxford, UK; Malden, USA : Munksgaard International Publishers
    Physiologia plantarum 123 (2005), S. 0 
    Details
    ISSN: 1399-3054
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Vacuolar processing enzyme (VPE) is a cysteine protease that has substrate specificity toward Asn and Asp residues, and found in various eukaryotic organisms including higher plants and mammals. Plant VPEs are separated into three subfamilies: seed-type, vegetative-type and uncharacterized-type. VPE was originally identified as a protease responsible for the maturation of seed storage proteins, and recent research has shown that it is a key protease responsible for the maturation of various vacuolar proteins not only in maturating cotyledons, but also in vegetative tissues. Thus, the VPE-mediated processing system is important for various vacuolar functions in the plant. Vegetative-type VPEs are expressed during senescence or pathogen-induced hypersensitive response. A VPE-deficiency abolished programmed cell death during hypersensitive response in tobacco leaves after TMV infection. This suggests that vegetative-type VPEs are involved in vacuolar-organized programmed cell death.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1399-3054.2005.00464.x
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  • 7
    Electronic Resource
    Electronic Resource
    Immunological analysis of aconitase in pumpkin cotyledons: the absence of aconitase in glyoxysomes (1994)
    Oxford, UK : Blackwell Publishing Ltd
    Physiologia plantarum 90 (1994), S. 0 
    Details
    ISSN: 1399-3054
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Aconitase (EC 4.2.1.3) was purified by column chromatography and SDS-PAGE. Specific antibodies for aconitase were prepared after affinity purification of the antiserum with purified aconitase. The antibodies reacted with purified pumpkin aconitase, and with the 98 kDa protein band after electrophoretic fractionation of extracts of pumpkin cotyledons. Immunoblot analysis revealed a protein with similar molecular mass in extracts of several plants. The intensity of the 98 kDa band increased as pumpkin cotyledons developed in darkness, and decreased thereafter upon illumination. Aconitase activity showed a similar pattern. Anion exchange chromatography of a homogenate of pumpkin cotyledons, followed by western blotting, displayed the presence of immunoreactive protein bands only in fractions showing aconitase activity. The results indicate that the antibodies were specific for aconitase. When we investigated the presence of immunoreactive bands after sucrose gradient fractionation, aconitase was detected in the supernatant fractions and in mitochondria, while a very low amount was found in glyoxysomes. These data provide additional proof that aconitase is not localized in glyoxysomes.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1399-3054.1994.tb02534.x
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  • 8
    Electronic Resource
    Electronic Resource
    Hydrolysis of protein in vacuoles isolated from higher plant tissue (1979)
    [s.l.] : Nature Publishing Group
    Nature 277 (1979), S. 412-413 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Fig. 1 Photomicrographs of a, protein bodies prepared from dry castor beans, and, 6, vacuoles prepared from endosperm of 4-d-old seedlings and purified by passage into 40% sucrose containing 0.1 mM EDTA . Bars, 50 |xm. Table 1 Protein content of protein bodies and vacuoles Protein ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/277412a0
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  • 9
    Electronic Resource
    Electronic Resource
    Microbody proliferation and segregation cycle in the single-microbody alga Cyanidioschyzon merolae (1999)
    Springer
    Planta 208 (1999), S. 326-336 
    Details
    ISSN: 1432-2048
    Keywords: Key words:Cyanidioschyzon ; Microbody ; Organelle proliferation ; Rhodophyta
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract. The proliferation cycle of the microbody was studied in the primitive red alga Cyanidioschyzon merolae, which contains one microbody per cell. Cells were synchronized with a dark/light cycle, and the morphology of the microbody and its interaction with other organelles were observed three-dimensionally by fluorescence microscopy, transmission electron microscopy, and computer-assisted three-dimensional reconstruction of serial thin sections. The microbody in interphase cells is a sphere of 0.3 μm in diameter without a core. In M-phase, the microbody passes through a series of irregular shapes, in the order rod, worm, branched, H-shaped and dumbbell, and symmetric fission occurs just before cytokinesis. The microbody duplicates its volume in M-phase and three-dimensional quantitative analysis revealed that its surface area increases before its volume does. The microbody touches the mitochondrion and the chloroplast throughout its proliferation cycle, except briefly in interphase cells, winding around the divisional plane of the mitochondrion at one phase. Immunocytochemical labeling of catalase as a marker of matrix proteins of the microbody revealed that the duplication of catalase occurs in tandem with the volume increase. While no specific apparatus was identified in the microbody divisional areas, we identified an electron-dense apparatus about 30–50 nm in diameter between the microbody and the mitochondrion that may play a role in segregating the daughter microbodies. These results are the first characterization to show the morphological changes of one microbody in a one-microbody alga without proliferation-inducing substrates, which have been used in many studies, and clearly show that two daughter microbodies arise by binary fission of the pre-existing microbody.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004250050566
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  • 10
    Electronic Resource
    Electronic Resource
    Molecular structure and subcellular localization of spinach leaf glycolate oxidase (1983)
    Springer
    Photosynthesis research 4 (1983), S. 99-109 
    Details
    ISSN: 1573-5079
    Keywords: antiserum ; glycolate oxidase ; leaf peroxisome ; spinach leaves ; photorespiration
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Glycolate oxidase (E.C. 1.1.3.1) was purified from spinach leaves (Spinacia oleracea). The molecular weight of the native protein was determined by sucrose density gradient centrifugation to be 290,000 daltons (13S), whereas that of the monomeric form was 37,000 daltons. The quaternary structure of the holoenzyme is likely to be octameric, analogous to pumpkin cotyledon glycolate oxidase [Nishimura et al, 1982]. The subcellular localization of the enzyme was studied using linear sucrose density gradient centrifugation, and it was found that glycolate oxidase activity is detectable in both leaf peroxisomal and supernatant fractions, but not in chloroplasts and mitochondria; the activity distribution pattern is essentially similar to that for catalase, a known leaf peroxisomal enzyme. Ouchterlony double diffusion and immunotitration analyses, demonstrated that the rabbit antiserum against purified spinach leaf glycolate oxidase cross-reacted, identically, with the enzyme molecules present in two different subcellular fractions, i.e, the leaf peroxisome and supernatant fractions. It is thus concluded that the enzyme present in the supernatant is due to the disruption of leaf peroxisomes during the isolation, and hence glycolate oxidase is exclusively localized in leaf peroxisomes in spinach leaves.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00052371
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