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  • 1
    Electronic Resource
    Electronic Resource
    Biogenesis of Glyoxysomes (1984)
    Palo Alto, Calif. : Annual Reviews
    Annual Review of Plant Physiology 35 (1984), S. 321-347 
    Details
    ISSN: 0066-4294
    Source: Annual Reviews Electronic Back Volume Collection 1932-2001ff
    Topics: Biology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1146/annurev.pp.35.060184.001541
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    A NOVEL ROLE FOR PEROXISOMES IN OILSEED DEVELOPMENT (1982)
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 386 (1982), S. 0 
    Details
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1749-6632.1982.tb21442.x
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  • 3
    Electronic Resource
    Electronic Resource
    Cytochemical localization of glycolate oxidase in microbodies (glyoxysomes and peroxisomes) of higher plant tissues with the CeCl3 technique (1981)
    Springer
    Protoplasma 108 (1981), S. 39-53 
    Details
    ISSN: 1615-6102
    Keywords: Crystalline inclusions ; Cytochemistry ; Glycolate oxidase ; Glyoxysomes ; Peroxisomes
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Alpha hydroxy acid oxidase activity (using glycolate as substrate) was demonstrated cytochemically in leaf-type peroxisomes, glyoxysomes, and unspecialized peroxisomes of higher plant tissues with the CeCl3 technique in which cerous ions react with enzyme-generated H2O2 to form insoluble, electron-dense cerium perhydroxide. In all peroxisomes examined, reaction product was deposited throughout the matrices. None of the three types of microbody inclusions (crystals, amorphous nucleoids, or fibrillar, threadlike structures) observed in leaftype peroxisomes showed cytochemical reactivity. However, results with crystal-containing peroxisomes of guayule and tobacco leaves indicate an intimate association of glycolate oxidase with the crystals; reaction product was deposited in the spaces between the structural units of the crystal. Prolonged (18- versus 3-hour) incubation with glycolate and CeCl3 were required for reliable cytochemical reactivity in glyoxysomes of castor bean endosperm and unspecialized peroxisomes of barley coleoptile, both of which contain relatively low enzyme activity. The CeCl3 procedure may prove useful for helping identify microbodies observed with the electron microscope as peroxisomes. The lack of significant background deposits, and resolution of reaction product within crystals, illustrate qualities of the CeCl3 procedure superior to those of the ferricyanide-reduction method, which was previously used to localize glycolate oxidase in higher plant microbodies.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01276882
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  • 4
    Electronic Resource
    Electronic Resource
    Protein A-gold immunocytochemistry of isocitrate lyase in cotton seeds (1985)
    Springer
    Protoplasma 124 (1985), S. 157-167 
    Details
    ISSN: 1615-6102
    Keywords: Glyoxysomes ; Gossypium ; Immunocytochemistry ; Isocitrate lyase ; Protein A-gold
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The protein A-gold technique with plastic-embedded sections was used to localize isocitrate lyase (ICL) in cotyledons of mature (50-day-postanthesis) and germinated (24 and 48 hours old) cotton (Gossypium hirsutum) seeds. This is the first report of an ultrastructural localization of a glyoxysomal enzyme by post-embeddment immunocytochemistry. Standard glutaraldehyde, post-osmium tetroxide (3%, 2%) fixation resulted in the retention of more ICL antigenicity in sections of germinated seeds than with aldehyde fixation alone. This became apparent only after overcoming the masking effect of osmium tetroxide on protein antigenicity by pretreatment of sections with sodium metaperiodate. The pattern of gold labeling showed that enzyme was distributed throughout the glyoxysomal matrix including amorphous nucleoid inclusions. Specific association of any enzyme with these structures has not been demonstrated before. Activity of ICL was not detectable spectrophotometrically in extracts or isolated organelles of mature embryos, whereas antigen was demonstrated immunocytochemically and by double immunodiffusion. These results, plus biochemical evidence from our previous work, established the presence of glyoxysomes with a complete complement of enzymes in mature seeds. The increase in ICL activity following germination was accompanied by an increase in density of gold particles over glyoxysomal matrices. Transformation of density values through stereological formulae to a hypothetical number of particles per glyoxysome revealed a 4-fold increase in immunocytochemical detectability which correlated with the 4-fold increase in enzyme activity between 24- and 48-hour post-imbibition. We were unable to detect a site of synthesis despite good ultrastructural preservation of polysomes, likely due to an extremely low concentration of nascent ICL molecules at any polysome when cell metabolism was terminated by fixation. Results of this study support the hypothesis developed in our laboratory that complete glyoxysomes are synthesized during cottonseed maturation, then enlarge and accumulate enzymes by post-translational additions from the cytosol for lipid mobilization during seedling growth.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01290766
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  • 5
    Electronic Resource
    Electronic Resource
    C-terminal polypeptides are necessary and sufficient for in vivo targeting of transiently-expressed proteins to peroxisomes in suspension-cultured plant cells (1996)
    Springer
    Protoplasma 195 (1996), S. 156-167 
    Details
    ISSN: 1615-6102
    Keywords: Chloramphenicol acetyltransferase ; Cotton ; Malate synthase ; Microprojectile bombardment ; Peroxisome targeting signals ; Suspension-cultured cells ; Tobacco
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The potential of tobacco BY-2 suspension-cultured cells for examining in vivo targeting and import of proteins into plant peroxisomes was shown recently in our laboratory. In the current study, the necessity and sufficiency of putative C-terminal targeting signals on cottonseed malate synthase and bacterial chloramphenicol acetyl-transferase (CAT) were examined in BY-2 cells. Cotton suspension cells also were evaluated as another in vivo peroxisome targeting system. Ultrastructural views of BY-2 cells showed that the peroxisomes were relatively small (0.1-0.3 μm diameter), a characteristic of so-called “unspecialized” peroxisomes, Peroxisomes in cotton and tobacco cells were identified with anti-cottonseed catalase IgGs as distinct immunofluorescent particles clearly distinguishable from abundant immunofluorescent mitochondria and plastids, marked with antibodies to β-ATPase and stearoyl-ACP Δ 9 desaturase, respectively. The C-terminal ser-lys-leu (SKL) motif is a well-established peroxisome targeting signal (PTS 1) for mammals and yeasts, but not for plants. Antiserum raised against SKL peptides recognized proteins only in peroxisomes in cotton and tobacco cells. The necessity of SKL-COOH for targeting of proteins to plant peroxisomes had not been demonstrated; we showed that SKL-COOH was necessary for directing cottonseed malate synthase to BY-2 peroxisomes. KSRM-COOH, a conservative modification of SKL-COOH, was shown by others to be sufficient for redirecting CAT in stably-transformed Arabidopsis plants to the leaf peroxisomes. Here we show with the same CAT constructs (e.g., pMON316CAT-KSRM) that KSRM is sufficient for targeting transiently-expressed passenger proteins to unspecialized BY-2 peroxisomes. These results provide new direct evidence for the necessity of SKL-COOH (a type 1 PTS) and sufficiency of a conservative modification of the PTS 1 (KSRM-COOH) for in vivo, heterologous targeting of proteins to plant peroxisomes.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01279194
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  • 6
    Electronic Resource
    Electronic Resource
    Glyoxylate cycle enzymes and catalase in digitonin-fractionated mitochondria inTurbatrix aceti (1978)
    Springer
    Protoplasma 94 (1978), S. 249-261 
    Details
    ISSN: 1615-6102
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The subcellular localization of the glyoxylate cycle enzymes, isocitrate lyase and malate synthase, and the peroxisomal marker, catalase, was examined in 14-day-old cultures of the nematodeTurbatrix aceti. Glyoxylate cycle enzymes co-sedimented with selected mitochondrial enzymes during rate sedimentation. Two separate enzyme peaks were resolved after isopycnic centrifugation on a sucrose gradient: glyoxylate cycle enzymes, isocitrate lyase and malate synthase, and the Krebs cycle markers, fumarase and citrate synthase, banded at a density of 1.214 g/cm3 while catalase consistently sedimented at 1.197 g/cm3. Electron microscopy revealed that mitochondria with similar morphology were the only recognizable organelles in both enzyme peaks. Notably, organelles resembling microbodies (glyoxysomes) were not present. The compartmentation of these enzymes within the mitochondria was examined by sequentially disrupting organelle membranes with varying concentrations of digitonin. The complete release of isocitrate lyase and malate synthase occurred concomitantly with the loss of matrix material from the mitoplasts. Citrate synthase was concurrently released, although to a lesser extent, while fumarase and catalase remained associated with disrupted membrane fragments at the highest concentration of digitonin used. Thus, glyoxylate cycle enzymes and catalase appear to be localized withinT. aceti mitochondria and not within glyoxysomes as generally found in other eucaryotes.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01276775
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  • 7
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    Biogenesis of Glyoxysomes (1984)
    Annual Reviews
    Details
    Publication Date: 1984-06-01
    Print ISSN: 0066-4294
    Topics: Biology
    Published by Annual Reviews
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