Library

X
feed icon rss

Your email was sent successfully. Check your inbox.

An error occurred while sending the email. Please try again.

Proceed reservation?

Export
  • 1
    Electronic Resource
    Electronic Resource
    Evolution of the nucleotide sequence of influenza virus RNA segment 7 during drift of the H3N2 subtype
    Amsterdam : Elsevier
    Gene 23 (1983), S. 233-239 
    Details
    ISSN: 0378-1119
    Keywords: Escherichia coli ; Molecular cloning ; restriction enzymes ; reverse transcriptase ; sequence determination ; spontaneous mutation
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology
    Type of Medium: Electronic Resource
    URL: http://linkinghub.elsevier.com/retrieve/pii/0378-1119(83)90055-0
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 2
    Electronic Resource
    Electronic Resource
    Cadmium induces senescence symptoms in leaf peroxisomes of pea plants (2001)
    Oxford, UK : Blackwell Science, Ltd
    Plant, cell & environment 24 (2001), S. 0 
    Details
    ISSN: 1365-3040
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: The effect of growing pea (Pisum sativum L.) plants with a toxic CdCl2 concentration (50 µm) on the metabolism and proteolytic activity of leaf peroxisomes was studied. In peroxisomes purified from plants treated with cadmium, an increase in the total protein concentration and in the activity and protein level of the photorespiratory enzyme glycolate oxidase was found. The glyoxylate cycle enzymes, malate synthase and isocitrate lyase, whose activity is normally very low in leaf peroxisomes, were enhanced by Cd treatment. The activity of the endogenous proteases of leaf peroxisomes was determined. Two leucine-aminopeptidase isozymes (AP1-AP2) were detected, and their activity was slightly higher in Cd-treated plants. Five endopeptidases (EP1-EP5) were present in pea leaf peroxisomes, and in plants grown with Cd the activity of isozymes EP1-EP4 was increased. The ultrastructural analysis of pea leaves showed that Cd produced a disorganization of the chloroplast structure, with an increase in the number of plastoglobuli, and the formation of vesicles in the vacuoles. Taken together, these results indicate that Cd induces senescence symptoms in leaf peroxisomes, and probably a metabolic transition of leaf peroxisomes into glyoxysomes, and suggest that the peroxisomal proteases could participate in the metabolic changes produced by Cd.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1365-3040.2001.00750.x
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 3
    Electronic Resource
    Electronic Resource
    Cadmium causes the oxidative modification of proteins in pea plants (2002)
    Oxford, UK : Blackwell Science Ltd
    Plant, cell & environment 25 (2002), S. 0 
    Details
    ISSN: 1365-3040
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: In pea (Pisum sativum L.) leaves from plants grown in the presence of 50 µm CdCl2 the oxidative production of carbonyl groups in proteins, the rate of protein degradation and the proteolytic activity were investigated. In leaf extracts the content of carbonyl groups measured by derivatization with 2,4-dinitrophenylhydrazine (DNPH), was two-fold higher in plants treated with Cd than in control plants. The identification of oxidized proteins was carried out by sodium dodecyl sulphate-polyacrylamide gel electrophoresis of proteins derivatized with DNPH and immunochemical detection with an antibody against DNPH. The intensity of the reactive bands was higher in plants exposed to Cd than in controls. By using different antibodies some of the oxidized proteins were identified as Rubisco, glutathione reductase, manganese superoxide dismutase, and catalase. The incubation of leaf crude extracts with increasing H2O2 concentrations showed a progressive enhancement in carbonyl content and the pattern of oxidized proteins was similar to that found in Cd-treated plants. Oxidized proteins were more efficiently degraded, and the proteolytic activity increased 20% due to the metal treatment. In peroxisomes purified from pea leaves a rise in the carbonyl content similar to that obtained in crude extracts from Cd-treated plants was observed, but the functionality of the peroxisomal membrane was not apparently affected by Cd. Results obtained demonstrate the participation of both oxidative stress, probably mediated by H2O2, and proteolytic degradation in the mechanism of Cd toxicity in leaves of pea plants, and they appear to be involved in the Cd-induced senescence previously reported in these plants.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1365-3040.2002.00850.x
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 4
    Electronic Resource
    Electronic Resource
    Mitochondrial and peroxisomal ascorbate peroxidase of pea leaves (1998)
    Copenhagen : Munksgaard International Publishers
    Physiologia plantarum 104 (1998), S. 0 
    Details
    ISSN: 1399-3054
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: The isoenzyme pattern and the substrate specificity of the membrane-bound mitochondrial and peroxisomal ascorbate peroxidases (APX; EC 1.11.1.11) from pea leaves are studied. The substrate specificity of both APXs was assayed using the electron donors ascorbate and pyrogallol, whereas o-dianisidine, hydroquinone, tetramethylbenzidine and 4-methoxy-α-naphthol were also assayed with mitochondrial APX (mitAPX). In leaf mitochondria, the specific activity of APX was similar with pyrogallol and ascorbate, the activity being inhibited by p-CMS. mitAPX showed low activity with the guaiacol peroxidase (GPX)-type substrates, tetramethylbenzidine and 4-methoxy-α-naphthol. Activity of mitAPX with hydroquinone suggest a potential role of mitAPX in the drainage of electrons from the mitochondrial electron chain at the level of ubiquinone. In peroxisomes, the APX (perAPX) specific activity was much higher with pyrogallol than with ascorbate. This perAPX was more sensitive to incubation with Triton X-100 than the mitAPX. By native PAGE the mitAPX was resolved in 6 isoenzyme bands, and the activity of the 3 main bands (mitAPX III, III′ and IV) was inhibited by p-CMS. These 3 major isozymes were also present in mitochondrial membrane fractions. Staining for GPX activity with 4-methoxy-α-naphthol revealed that the APX detected in mitochondria did not have the capacity to oxidize 4-MN, and therefore cannot be considered as true GPX. When intact peroxisomes and peroxisomal membranes were subjected to native PAGE, no APX activity could be detected and this was probably due to the inactivation of perAPX. Results obtained suggest that pea mitochondrial APX (mitAPX) represent a distinct and novel isozyme different from those APXs of chloroplast and cytosolic origin previously reported. The peroxisomal APX (perAPX), however, appears to ressemble the chloroplast APXs as regards its sensitivity to Triton X-100.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1034/j.1399-3054.1998.1040424.x
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 5
    Electronic Resource
    Electronic Resource
    Cadmium-induced subcellular accumulation of O2·− and H2O2 in pea leaves (2004)
    Oxford, UK : Blackwell Science Ltd
    Plant, cell & environment 27 (2004), S. 0 
    Details
    ISSN: 1365-3040
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Cadmium is a toxic metal that produces disturbances in plant antioxidant defences giving rise to oxidative stress. The effect of this metal on H2O2 and O2·− production was studied in leaves from pea plants growth for 2 weeks with 50 µm Cd, by histochemistry with diaminobenzidine (DAB) and nitroblue tetrazolium (NBT), respectively. The subcellular localization of these reactive oxygen species (ROS) was studied by cytochemistry with CeCl3 and Mn/DAB staining for H2O2 and O2·−, respectively, followed by electron microscopy observation. In leaves from pea plants grown with 50 µm CdCl2 a rise of six times in the H2O2 content took place in comparison with control plants, and the accumulation of H2O2 was observed mainly in the plasma membrane of transfer, mesophyll and epidermal cells, as well as in the tonoplast of bundle sheath cells. In mesophyll cells a small accumulation of H2O2 was observed in mitochondria and peroxisomes. Experiments with inhibitors suggested that the main source of H2O2 could be a NADPH oxidase. The subcellular localization of O2·− production was demonstrated in the tonoplast of bundle sheath cells, and plasma membrane from mesophyll cells. The Cd-induced production of the ROS, H2O2 and O2·−, could be attributed to the phytotoxic effect of Cd, but lower levels of ROS could function as signal molecules in the induction of defence genes against Cd toxicity. Treatment of leaves from Cd-grown plants with different effectors and inhibitors showed that ROS production was regulated by different processes involving protein phosphatases, Ca2+ channels, and cGMP.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-3040.2004.01217.x
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 6
    Electronic Resource
    Electronic Resource
    Reactive oxygen species-mediated enzymatic systems involved in the oxidative action of 2,4-dichlorophenoxyacetic acid (2004)
    Oxford, UK : Blackwell Science Ltd
    Plant, cell & environment 27 (2004), S. 0 
    Details
    ISSN: 1365-3040
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: 2,4-dichlorophenoxyacetic acid (2,4-D) is an analogue compound to the plant hormone indole-3-acetic acid (IAA), which is used either as a growth-promoting substance or as a herbicide, depending on its concentration. In this work, the effect of 2,4-D on the growth and ROS metabolism of pea (Pisum sativum L.) leaves is reported. The herbicide considerably reduced the plant growth and negatively influenced several physiological parameters in a dose-dependent manner. At structural level, damage of the mesophyll cells and the enlargement and dilation of thylakoids were observed in 2,4-D-treated plants. 2,4-D notably affected xanthine oxidase and superoxide dismutase activities, as well as the activity and transcript levels of the ascorbate–glutathione cycle enzymes, ascorbate peroxidase, monodehydroascorbate reductase, and glutathione reductase. Furthermore, in herbicide-treated plants, an increase in the H2O2 production, levels of lipid peroxidation, endopeptidase activity and oxidatively modified proteins took place. Results obtained showed that an overproduction of superoxide radicals (O2−) and hydrogen peroxide (H2O2) could take place in plants treated with 2,4-D, thus contributing to the generation of oxidative stress, with the concomitant degradation of proteins. A model of the role of ROS-mediated enzymatic systems in the oxidative mode of action of 2,4-D and other auxinic herbicides is proposed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-3040.2004.01219.x
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...