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  • 1
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 44 (1987), S. 0 
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Cyanophycin is a high molecular weight co-polymer of aspartate and arginine, hitherto considered characteristic of all cyanobacteria. Chemical analysis and radioisotopic incorporation procedures have shown that precipitable cyanophycin is absent from the five species of Synechococcus tested, including the marine Synechococcus WH7803 (type DC2). The implications with respect to the role of cyanobacterial nitrogen reserves are discussed.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract Three constitutive forms of Superoxide dismutase activity have been demonstrated in the cyanobacterial marine picoplankter Synechococcus sp. WH 7803 using polyacrylamide gel activity staining techniques. A protein which gave a positive non-haem iron stain on native polyacrylamide gels exhibited N-terminal similarity to both the iron Superoxide dismutase and the manganese Superoxide dismutase of Escherichia coli. The metal prosthetic group of each of the three activity bands was characterised by analysing their differential sensitivities to 5 mM H2O2, 2 mM cyanide and 2 mM of the copper chelator diethyldithiocarbamate. Three distinct Superoxide dismutase activities were observed, an iron Superoxide dismutase, a copper/zinc Superoxide dismutase and a third form which has not been identified. Growth of Synechococcus cells in ASW medium containing no added iron resulted in no alteration in the activity of the iron Superoxide dismutase. Growth of cultures in the absence of copper or zinc resulted in differential changes in the activities of the copper/zinc Superoxide dismutase and the unidentified Superoxide dismutase.
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract The region of the genome encoding the glucose-6-phosphate dehydrogenase gene zwf was analysed in a unicellular cyanobacterium, Synechococcus sp. PCC 7942, and a filamentous, heterocystous cyanobacterium, Anabaena sp. PCC 7120. Comparison of cyanobacterial zwf sequences revealed the presence of two absolutely conserved cysteine residues which may be implicated in the light/dark control of enzyme activity. The presence in both strains of a gene fbp, encoding fructose-1,6-bisphosphatase, upstream from zwf strongly suggests that the oxidative pentose phosphate pathway in these organisms may function to completely oxidize glucose 6-phosphate to CO2. The amino acid sequence of fructose-1,6-bisphosphatase does not support the idea of its light activation by a thiol/disulfide exchange mechanism. In the case of Anabaena sp. PCC 7120, the tal gene, encoding transaldolase, lies between zwf and fbp.
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  • 4
    ISSN: 1573-5028
    Keywords: Synechococcus ; glucose-6-phosphate dehydrogenase ; cyanobacterium
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The glucose-6-phosphate dehydrogenase (EC 1.1.1.49) gene (zwf) of the cyanobacterium Synechococcus PCC 7942 was cloned on a 2.8 kb Hind III fragment. Sequence analysis revealed an ORF of 1572 nucleotides encoding a polypeptide of 524 amino acids which exhibited 41% identity with the glucose-6-phosphate dehydrogenase of Escherichia coli.
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  • 5
    ISSN: 1573-5028
    Keywords: Synechococcus sp. WH7803 ; phycocyanin ; picoplankton ; cyanobacteria
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Type of Medium: Electronic Resource
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  • 6
    ISSN: 1573-5028
    Keywords: phycoerythrin ; Synechococcus sp. WH7803 ; picoplankton ; marine cyanobacteria
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The nucleotide sequences of the class I phycoerythrin (PE) α-and β-subunit genes (cpeA and cpeB) from the marine cyanobacterium Synechococcus sp. WH7803 are reported. The cpeB gene is located upstream of cpeA with a separation of 56 nucleotides and the two genes are co-transcribed as a transcript of 1.3 kb, with the transcription startpoint being localized to 110–111 bp upstream of cpeB. The sequence of the promoter region bears no similarity to promoters reported for other cyanobacterial PE genes. Pentanucleotide repeats found upstream of some PE operons, particularly in the case of cyanobacterial strains capable of chromatic adaption, are not found in Synechococcus sp. WH7803; instead the sequence 5′-CGGTT-3′ is repeated three times in the promoter region.
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  • 7
    Electronic Resource
    Electronic Resource
    Springer
    Molecular and cellular biochemistry 66 (1985), S. 151-162 
    ISSN: 1573-4919
    Keywords: cytosol and smooth endoplasmic reticulum ; multiple forms ; synthase phosphatase and phosphorylase phosphatase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Summary The smooth endoplasmic reticulum (ER) and cytosol fractions of liver homogenates exhibit phosphoprotein phosphatase activity towards glycogen synthase D and phosphorylase a. The following observations suggest that liver contains multiple forms of these phosphatases. Synthase phosphatase activity in either fraction was more readily inactivated by heating than phosphorylase phosphatase activity. Both synthase phosphatase and phosphorylase phosphatase activities in smooth ER were non-competitively inhibited by Mg2+, but were activated by this ion in the cytosol. Synthase phosphatase activities in cytosol and smooth ER were stimulated by a number of sugar phosphates, particularly glucose-l-phosphate, galactose-6-phosphate and fructose-6-phosphate. Erythrose-4-phosphate stimulated synthase phosphatase activity in the cytosol, but inhibited the microsomal enzyme. Phosphorylase phosphatase activities in either fraction were inhibited by most sugar phosphates. Adenosine mono-, di- and tri-phosphates inhibited phosphatase activities in both fractions. Low concentrations of AMP and ADP inhibited phosphorylase phosphatase activities to a greater extent than synthase phosphatase activities. Chromatography of the smooth ER fraction on DEAE-cellulose resulted in the separation of synthase phosphatase from phosphorylase phosphatase, as soluble proteins. The elution profile for the microsomal phosphatase was different from that for the cytosol enzymes. It is concluded that: (a) both synthase phosphatase and phosphorylase phosphatase in liver have at least two isoenzyme forms (b) synthase phosphatase and phosphorylase phosphatase are separate enzymes (c) the different behaviour of microsomal and cytosol phosphatases towards divalent cations and sugar phosphates provides a potential mechanism for the differential regulation of these activities in liver.
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  • 8
    Electronic Resource
    Electronic Resource
    Springer
    Molecular and cellular biochemistry 74 (1987), S. 95-101 
    ISSN: 1573-4919
    Keywords: phosphoprotein phosphatases ; growth hormone peptides ; phosphorylase ; glycogen synthase ; protein kinase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Abstract The N-terminal part sequences of pituitary growth hormone, Nα-acetyl-hGH 7–13 and hGH 6–13, promoted conversion of glycogen synthase b to glycogen synthase a in skeletal muscle and adipose tissue when injected intravenously. The peptides also caused conversion of phosphorylase a to phosphorylase b in liver and adipose tissue, but not in muscle, where the peptides antagonised activation of phosphorylase. Synthase phosphatase activity in muscle and phosphorylase phosphatase activity in liver increased after injection of peptide, with time courses of change similar to those seen for muscle synthase and liver phosphorylase activities. Injection of peptide also decreased both the cyclic AMP dependent and independent synthase kinase activities in muscle. These results show that the insulin-like activities of these peptides on glycogen synthase and phosphorylase involve both increases in protein phosphatase activities and inhibition of protein kinase activities. These results are discussed in relation to the insulin-like activities of growth hormone.
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  • 9
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    MDPI - Multidisciplinary Digital Publishing Institute
    Publication Date: 2024-03-29
    Description: Higher education institutions (HEIs) have a unique role and responsibility for the future and for driving the development of a sustainable society. HEIs are charged with the task of fostering sustainability in the leaders of tomorrow, developing solutions and methods for addressing a sustainable future and ensuring that knowledge is contributed to society. HEIs must also ensure that their everyday operations and practices are consistent with a sustainable future, and that they work toward holistically integrating sustainability into both the mission of a university and its daily tasks. This Special Issue builds on papers presented during the 2018 International Sustainable Campus Network Conference and also includes other contributions. The articles reflect the many aspects of sustainability in higher education institutions and illustrate innovation in approach, outcomes, and impact. The papers cover a range of perspectives on sustainability both on and around campuses. These include organization and management issues, networking and city partnership themes, and metrics and indicators related to sustainable development goals. The Special Issue also includes papers on education, student involvement, and gender issues. Select articles include results from surveys and desktop research; others depict approaches on experimentation, living labs, and action research.
    Keywords: L7-991 ; H1-99 ; management model ; cities´ decarbonization ; sustainable development goals ; keyword search ; universities ; sustainability in higher education ; wellbeing ; sustainable energy ; education for sustainability (EfS) ; sustainable modes of transportation ; sustainable environment ; living lab ; Campus ; Education for Sustainable Development ; willingness to use ; whole institution approach ; impacts ; sustainability reporting ; water bottle refill stations ; academic organizational change ; transdisciplinarity ; SDGs ; contingent valuation method ; gender ; sustainability solutions ; Research ; leaky pipeline ; networks ; organizational change ; university campus ; sustainable university ; behavioral change ; institutional design ; community partnership ; innovation ; sustainability assessment ; higher education institution ; change drivers ; curriculum innovation ; university cooperation ; social innovation ; academic career ; interdisciplinarity ; equal opportunities ; grand challenges ; transportation ; campus sustainability ; participatory action research ; CO2 emissions ; European Union ; collaboration ; prefigurative politics ; undergraduate ; public university ; governance ; circularity ; sustainability course inventory ; global south ; environmental footprint mitigation ; agent of change ; zero carbon cities ; responsible science ; macro-universities ; sustainability indicators ; campus development ; discrimination ; Sustainable Development Goals ; UNAM ; barriers to change ; cities ; sustainable development goals and universities ; Higher Education Institutions ; EMU ; sustainability ; sustainable development ; circular economy ; smart cities ; city–university partnerships ; smart city ; education for sustainable development (ESD) ; willingness to pay ; student engagement ; sustainable development in higher education institutions (SD in HEI) ; transformative learning ; university ; area development ; education for sustainable development ; learning ; faculty empowerment ; university living lab ; regenerative approach ; research database ; higher education ; air travel ; agenda 2030 ; carbon footprint ; higher education institutions ; capacity-building ; Mexico ; sustainability assessment tools ; critical case study ; age ; bic Book Industry Communication::J Society & social sciences::JN Education ; thema EDItEUR::J Society and Social Sciences::JN Education
    Language: English
    Format: application/octet-stream
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  • 10
    Publication Date: 2007-10-08
    Description: There is abundant field and microstructural evidence for localization of deformation in alpine- and ophiolite-type mantle massifs. On the basis of field relationships and microstructures we recognize two types of tectonite shear zones (medium- to coarse- and fine-grained), as well as two types of mylonitic shear zones (anhydrous and hydrous peridotite mylonites). In tectonite shear zones, softening processes responsible for localization are probably melt-related weakening in the medium to coarse tectonites and a change in limiting slip system in the fine-grained tectonites. In peridotite mylonites, the most likely cause for softening and localization is a change in dominant deformation mechanism from dislocation to grain size sensitive creep. Microstructural and petrological study of mylonite rocks reveals that reactions, either continuous net-transfer reactions (anhydrous and hydrous) or melt-rock reactions, play a key role in the formation of fine-grained material that promotes grain size sensitive creep. These reactions occur over a broad range of pressure-temperature conditions encompassing a large part of the lithospheric upper mantle. We conclude that mantle shear zones are widespread and that they reduce the (bulk) strength of the lithosphere significantly.
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