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1

Electronic Resource

Localization of Glyoxylate Cycle Enzymes in Glyoxysomes in Euglena (1972)

GRAVES, LYNN B. ; TRELEASE, RICHARD N. ; GRILL, ALBIN ; [et al.]

Oxford, UK : Blackwell Publishing Ltd

The @journal of eukaryotic microbiology 19 (1972), S. 0

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ISSN: 1550-7408

Source: Blackwell Publishing Journal Backfiles 1879-2005

Topics: Biology

Notes: SYNOPSIS. We demonstrated previously microbodies in Euglena gracilis grown in the dark on 2-carbon substrates. We have now established in Euglena the particulate nature of enzymes known in other organisms to be localized in microbodies (glyoxysomes and leaf peroxisomes). On a linear sucrose gradient the glyoxylate cycle enzymes band together at a nigner equilibrium density (1.20 g/cm3) than mitochondrial marker enzymes (1.17 g/cm3), establishing the existence in Euglena of glyoxysomes similar to those of higher plants. Glyoxylate (hydroxypyruvate) reductase and, under certain conditions, also glycolate dehydrogenase co-band with the glyoxylate cycle enzymes, suggesting that Euglena glyoxysomes, like those of higher plants, may contain peroxisomal-type enzymes. Catalase, an enzyme characteristic of microbodies from a variety of sources, was not detected in Euglena.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1111/j.1550-7408.1972.tb03521.x

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2

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Biochemical, electrophoretic and immunological characterization of peroxisomal enzymes in three soybean organs (1987)

Stegink, Steven J. ; Vaughn, Kevin C. ; Kunce, Christine M. ; [et al.]

Oxford, UK : Blackwell Publishing Ltd

Physiologia plantarum 69 (1987), S. 0

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ISSN: 1399-3054

Source: Blackwell Publishing Journal Backfiles 1879-2005

Topics: Biology

Notes: Biochemical, electrophoretic and immunological studies were made among peroxisomal enzymes in three organs of soybean [Glycine max (L.) Merr. cv. Centennial] to compare the enzyme distribution and characteristics of specialized peroxisomes in one species. Leaves, nodules and etiolated cotyledons were compared with regard to several enzymes localized solely in their peroxisomes: catalase (EC 1.11.1.6), malate synthase (EC 4.1.3.2), glycolate oxidase (EC 1.1.3.1), and urate oxidase (EC 1.7.3.3). Catalase activity was found in all tissue extracts. Electrophoresis on native polyacrylamide gels indicated that leaf catalase migrated more anodally than nodule or cotyledon catalase as shown by both activity staining and Western blotting. Malate synthase activity and immunologically detectable protein were present only in the cotyledon extracts. Western blots of denaturing (lithium dodecyl sulfate) gels probed with anti-cotton malate synthase antiserum, reveal a single subunit of 63 kDa in both cotton and soybean cotyledons. Glycolic acid oxidase activity was present in all three organs, but ca 20-fold lower (per mg protein) in both nodule and cotyledon extracts compared to leaf extracts. Electrophoresis followed by activity staining on native gels indicated one enzyme form with the same mobility in nodule, cotyledon and leaf preparations. Urate oxidase activity was found in nodule extracts only. Native gel electrophoresis showed a single band of activity. Novel electrophoretic systems had to be developed to resolve the urate oxidase and glycolate oxidase activities; both of these enzymes moved cathodally in the gel system employed while most other proteins moved anodally. This multifaceted study of enzymes located within three specialized types of peroxisomes in a single species has not been undertaken previously, and the results indicate that previous comparisons between the enzyme content of specialized peroxisomes from different organisms are mostly consistent with that for a single species, soybean.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1111/j.1399-3054.1987.tb04278.x

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3

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Purification of plant peroxisomes in iso-osmotic metrizamide (1990)

Turley, Rickie B. ; Trelease, Richard N.

Oxford, UK : Blackwell Publishing Ltd

Physiologia plantarum 79 (1990), S. 0

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ISSN: 1399-3054

Source: Blackwell Publishing Journal Backfiles 1879-2005

Topics: Biology

Notes: Methods were developed for isolating highly-purified peroxisomes under iso-osmotic conditions from 3 plant parts, namely cotyledons of cotton (Gossypium hirsutum L.) seedlings, endosperm of castor bean (Ricinus communis L.) seedlings and leaves of mature spinach (Spinaca oleracea L.) plants. Purification was achieved by sedimentation of the organelles into metrizamide gradients centrifuged in a vertical rotor (VTi 50). Gradients consisted of an upper transition layer (1:1 mixture of homogenizing medium and 0.25 M metrizamide), a linear 0.25–0.76 M metrizamide gradient and a 0.76 M metrizamide pad. Peroxisomes from all 3 plant parts were recovered in a major band at a density ranging from 1.24 to 1.27 g cm−3, which is a density range similar to that for peroxisomes isolated in sucrose gradients. The percent of the total gradient cytochrome c oxidase (mitochondria marker) activity recovered in peroxisome fractions ranged from 1.5% in endosperm to 2.8% in leaves, while a plastid marker (chlorophyll or galactosyl transferase activity) ranged from undetectable in leaf peroxisome fractions to 3.6% in endosperm peroxisome fractions. Intactness of the peroxisomes was judged to be 69%, 89% and 78% for the cotyledon, endosperm and leaf peroxisomes, respectively. Isolated peroxisomes were stable for at least 5 h in metrizamide medium. Microscopic (bright-field and transmission electron microscopy) assessments verified that the peroxisomes were morphologically intact and fractions were essentially free of contaminating organelles. Metrizamide is an excellent iso-osmotic medium for purifying peroxisomes from these plant organs and tissue.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1111/j.1399-3054.1990.tb02119.x

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4

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The occurrence and fine structural characterization of microbodies inEuglena gracilis (1971)

Graves, Lynn B. ; Hanzely, Laszlo ; Trelease, Richard N.

Springer

Protoplasma 72 (1971), S. 141-152

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ISSN: 1615-6102

Source: Springer Online Journal Archives 1860-2000

Topics: Biology

Notes: Summary The fine structure of an organelle morphologically similar to microbodies found in higher plants and animals was studied in cells ofEuglena gracilis fixed simultaneously in glutaraldehyde and osmium tetroxide. These organelles were 0.4 to 0.8 microns in diameter, bounded by a single membrane, and frequently observed in close spatial association with both endoplasmic reticulum and mitochondria. Their finely granular matrices frequently contained membranous cores. Though these organelles were relatively abundant in acetate- and ethanolgrown cells, they were rarely observed in glucose-grown cells, an indication that they play the same role in the metabolism of 2-carbon substrates as do glyoxysomes in higher plants. The presence of these organelles, assumed to be microbodies, is also of considerable interest since catalase, an enzyme characteristic of microbodies from a variety of sources, was not detected.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1007/BF01279047

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5

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Metabolism of carbohydrate and lipid reserves in germinated cotton seeds (1982)

Doman, Diane C. ; Walker, John C. ; Trelease, Richard N. ; [et al.]

Springer

Planta 155 (1982), S. 502-510

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ISSN: 1432-2048

Keywords: Carbohydrate metabolism ; Gluconeogenesis ; Gossypium ; Lipid utilization ; Raffinose ; Starch synthesis

Source: Springer Online Journal Archives 1860-2000

Topics: Biology

Notes: Abstract Utilization of reserve lipid and carbohydrates during germination (0–12 h) and postgerminative growth (12–48 h) was studied in cotton (Gossypium hirsutum L.) seedlings. Raffinose and stachyose were utilized during the germination period and early growth; mobilization was associated with α-galactosidase (EC 3.2.1.22) activity. Results from pulse-chase experiments with [3H]raffinose supplied exogenously to 4-h soaked seeds indicated that raffinose-derived catabolites contributed to the coincident increase in cotyledon sucrose and starch, and to the small increase in axis dry weight. Starch appears to be an alternative sink for end products of hydrolysis of reserve carbohydrates prior to the onset of rapid axis growth and cotyledon expansion. Mobilization of neutral lipid commenced at about 16 h after soaking, concomitant with development of key glyoxylate-cycle and other gluconeogenesis-related enzyme activities. Axis dry weight increased three-fold between 24 and 48 h. Results from pulse-chase (3 h, 16 h) experiments in which [2-14C]acetate was supplied to cotyledons of intact 22-h-old seedlings showed that acetate-derived metabolites were not transported exclusively to the axes, but were partitioned between axes and cotyledons. Only 27% of total incorporated radioactivity was recovered in axes following the chase, 18% was evolved as CO2, and the rest was recovered in water-soluble substances (20%) and polymers (31%) within the cotyledons. Of the polymers, 55% of the activity was in polysaccharides (Starch, pectic substances, hemicellulose, cellulose), 25% in protein, and 20% in unidentified neutral and acidic compounds. Considering these data, the amount of lipid mobilized, and various routes by which supplied [2-14C]acetate could be metabolized, it appears that lipidderived compounds contribute only 25–40% of axis dry-weight gain. Lipid-derived substances retained in the cotyledons likely are utilized for expansion and differentiation of the cotyledons into photosynthetic organs.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1007/BF01607574

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6

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A correlative ultrastructural and enzymatic study of cotyledonary microbodies following germination of fat-storing seeds (1970)

Gruber, Peter J. ; Trelease, Richard N. ; Becker, Wayne M. ; [et al.]

Springer

Planta 93 (1970), S. 269-288

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ISSN: 1432-2048

Source: Springer Online Journal Archives 1860-2000

Topics: Biology

Notes: Summary Sunflower, cucumber, and tomato cotyledons, which contain microbodies in both the early lipid-degrading and the later photosynthetic stages of post-germinative growth, were processed for electron microscopy according to conventional procedures and examined 1, 4 and 7 days after germination. Homogenates of sunflower cotyledons were assayed for enzymes characteristic of glyoxysomes and leaf peroxisomes (both of which are defined morphologically as microbodies) at stages corresponding to the fixations for electron microscopy. The particulate nature of these enzymes was demonstrated by differential and equilibrium density centrifugation, making it possible to relate them to the microbodies seen in situ. One day after germination, the microbodies are present as small organelles among large numbers of protein and lipid storage bodies; the cell homogenate contains catalase but no detectable isocitrate lyase (characteristic of glyoxysomes) or glycolic acid oxidase (characteristic of leaf peroxisomes). 4 days after germination, numerous microbodies (glyoxysomes) are in extensive and frequent contact with lipid bodies. The microbodies often have cytoplasmic invaginations. At this stage the cells are rapidly converting lipids to carbohydrates, and the homogenate has high isocitrate lyase activity. 7 days after germination, microbodies (peroxisomes) are appressed to chloroplasts and frequently squeezed between them in the green photosynthetic cells. The homogenate at this stage has substantial glycolic acid oxidase activity but a reduced level of isocitrate lyase. It is yet to be determined whether the peroxisomes present at day 7 are derived from preexisting glyoxysomes or arise as a separate population of organelles.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1007/BF00384101

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7

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Control of enzyme activities in cotton cotyledons during maturation and germination (1981)

Choinski, John S. ; Trelease, Richard N. ; Doman, Diane C.

Springer

Planta 152 (1981), S. 428-435

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ISSN: 1432-2048

Keywords: Abscisic acid ; Embryo culture ; Gossypium ; Isocitrate lyase ; Malate synthase ; Seed maturation

Source: Springer Online Journal Archives 1860-2000

Topics: Biology

Notes: Abstract Cotton (Gossypium hirsutum L.) embryos excised from bolls 38–43 d after anthesis and cultured in vitro for 4 d on a nutrient agar medium containing 3.8 μM abscisic acid (ABA) developed enzyme activity and accumulated insoluble protein, neutral lipid, and dry weight similar to embryos maturing on the plant. Inclusion of ABA in the medium prevented precosious germination and allowed continued increases in catalase, malate dehydrogenase, citrate synthase, aspartate aminotransferase, and β-oxidation enzyme activities as well as de-novo synthesis of malate synthase. Isocitrate lyase activity was not detectable in ABA-cultured embryos nor normally-developed embryos. Omission of sucrose from the medium resulted in near-doubling of the development of malate synthase activity, with minimal effects on the other enzyme activities. Addition of Actinomycin D, cordycepin, or cycloheximide to ABA-containing cultures did not overcome the observed inhibition of germination, but severely reduced both the appearance of new malate synthase activity and further production of other related enzyme activities. Thus, development of these enzyme activities in the presence of ABA appears dependent on transcription and translation, while inhibition of germination by ABA at this stage of development is not sensitive to the RNA- and protein-synthesis inhibitors. The results indicate that ABA does not prevent vivipary by suppressing translation of m-RNAs coding for isocitrate lyase and its companion enzymes, as previously proposed.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1007/BF00385359

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8

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Ontogeny of glyoxysomes in maturing and germinated cotton seeds—a morphometric analysis (1984)

Kunce, Christine M. ; Trelease, Richard N. ; Doman, Diane C.

Springer

Planta 161 (1984), S. 156-164

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ISSN: 1432-2048

Keywords: Catalase ; Glyoxysome development ; Gossypium (glyoxysomes) ; Morphometry (glyoxysome development) ; Seed maturation

Source: Springer Online Journal Archives 1860-2000

Topics: Biology

Notes: Abstract Morphometric procedures were used with light and electron microscopy to examine glyoxysome number, volume, shape and distribution as well as mesophyll cell volume, in cotyledons of mature (50 d postanthesis), imbibed (5h) and germinated (24 and 37 h) cotton (Gossypium hirsutum L.) seeds. Additionally, activities of five glyoxysomal marker enzymes in cotyledon extracts were assayed at each of the above ages. Cell volume was determined from photomicrographs of Epon-embedded sections by the point-counting procedure. Analysis of variance showed that cell volume was not different among the tissue segments studied. Glyoxysomes were cytochemically stained for catalase (EC 1.11.1.6) activity with the 3,3′-diaminobenzidine-tetrahydrochloride procedure. Analyses involving both phase and electron microscopy, and two separate sterologic calculations for determining the number of glyoxysomes per cell, indicate that glyoxysomes are numerous in mature seeds, persist through desiccation and imbibition, then increase dramatically in volume (seven fold) but not number (a maximum of 1.5-fold), when enzyme activities increase two to six times (depending on the enzyme). During the entire period of increase in glyoxysomal enzyme activities, no ultrastructural evidence was found for glyoxysome formation or destruction. Our data, in contrast to some proposals in the literature, indicate that cottonseed glyoxysomes form during seed maturation, then develop following seed imbibition into pleomorphic organelles by posttranslational accumulation of proteins from the cytosol and transfer of membrane components probably from the endoplasmic reticulum.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1007/BF00395476

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9

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Development and regulation of three glyoxysomal enzymes during cotton seed maturation and growth (1990)

Turley, Rickie B. ; Trelease, Richard N.

Springer

Plant molecular biology 14 (1990), S. 137-146

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ISSN: 1573-5028

Keywords: catalase ; glyoxysomes ; Gossypium hirsutum ; isocitrate lyase ; malate synthase ; seed maturation

Source: Springer Online Journal Archives 1860-2000

Topics: Biology

Notes: Abstract The temporal, nonconcerted development of activities of malate synthase (MS), isocitrate lyase (ICL), and catalase (Cat) was explored in more detail in maturing and germinated cotton (Gossypium hirsutum L.) seeds. RNA was extracted at six intervals beginning at 17 days post anthesis (DPA) through 72 hours post imbibition (HPI). In vitro translations revealed that mRNAs for each enzyme were translatable at all intervals. Enzyme activities and immunoselected proteins also were found at all intervals. Similar specific activities throughout maturation indicated that embryo cells were not accumulating inactive protein. The steady-state level of mRNAs encoding each enzyme exhibited different patterns of change during seed maturation, and each peaked at least 24 h before peak enzyme activities in germinated seeds. All three enzymes occur together as early as 17 DPA in a coordinate manner; however, the subsequent, nonconcerted increases in protein, activity, and mRNA for each enzyme indicate that developmental expression in cotton seed embryos is regulated in a noncoordinate fashion by as yet unidentified specific control mechanism(s).

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1007/BF00018555

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