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  • 1
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Biochemistry 29 (1990), S. 9203-9211 
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Archives of microbiology 139 (1984), S. 299-304 
    ISSN: 1432-072X
    Keywords: Hydrogenase ; Regulatory mutants ; Formate hydrogen-lyase ; Escherichia coli ; hyd::lac fusion
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The regulation of synthesis of the hydrogenase which is a component of the formate hydrogen-lyase complex was studied by means of a strain of Escherichia coli possessing a transcriptional fusion of the hydrogenase gene (hyd) with the lacZ gene (hyd::lac fusion). Formation of active hydrogenase in the wild strain requires the presence of nickel in the medium; transcription of the hyd gene, however, is independent from the prescence of Ni2+. Ni2+ addition to Ni2+-prestarved cells did not lead to any activation of presumptive hydrogenase apoprotein. Regulatory mutants were isolated in which nitrate repression of hyd::lac expression was relieved. Two main classes of regulatory mutants were identified: (i) Mutants with a defect in nitrate reductase; (ii) mutants with a cis-dominant regulatory mutation closely linked to the hyd::lac fusion. In the presence of formate which acts as an inducer, the hyd::lac fusion was also expressed under aerobic conditions. The results infer that nitrate repression of transcription of the hydrogenase structural gene is not effected by nitrate itself but requires the function of the electron transport chain leading to nitrate and that mutations in the promoter/operator region of the hyd cistron may confer insensitivity to redox control both by oxygen and nitrate.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Springer
    Archives of microbiology 141 (1985), S. 359-363 
    ISSN: 1432-072X
    Keywords: Escherichia coli ; Phage Mu d, formic dehydrogenase ; Seleno-polypeptide ; Respiratory pathway
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The site of integration of phage Mu d (Ap lac) in mutant M9s which leads to deficiency of formic dehydrogenase (benzylviologen-linked) activity was determined. It was shown that the phage had inserted into the gene for the seleno-polypeptide of the enzyme (80 kd) leading to the formation of a truncated peptide (60 kd) still able to incorporate Se. Synthesis of the truncated polypeptide is subject to the same regulatory signals as that of the wild-type enzyme. The formation of the 110 kd seleno-polypeptide, which is a constituent component of the formic dehydrogenase from the formate-nitrate respiratory pathway, is unimpaired in mutant M9s. The location of the gene for the 80 kd seleno-polypeptide was mapped at 92.4 min of the Escherichia coli chromosome.
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  • 4
    Electronic Resource
    Electronic Resource
    Springer
    Archives of microbiology 132 (1982), S. 365-371 
    ISSN: 1432-072X
    Keywords: Pyruvate formate-lyase ; Anaerobiosis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract It is shown here that a plasmid (p29) derived from the transducing phage λaspC2 (Christiansen and Pedersen 1981) codes for pyruvate formate-lyase. The identity of the 80 kilodaltons (kd) gene product of plasmid p29 with the pyruvate formate-lyase polypeptide was proven (i) by comigration of the gene product expressed in the maxicell system with purified enzyme on O'Farrell gels, and (ii) by comparison of the peptide maps obtained from limited proteolysis. In vivo the 80 kd form of the enzyme was proteolytically converted to a 78 kd polypeptide. The two polypeptides (80 kd and 78 kd) and their charge isomers present in purified enzyme preparations are therefore products of a single gene. Aerobically grown cells of Escherichia coli contained a basal level of pyruvate formate-lyase which was derepressed 5-to 10-fold under anaerobiosis. Derepression also occurred during anaerobic growth on glycerol plus fumarate. Presence of plasmid p29 caused overproduction of pyruvate formatelyase, 11-fold upon anaerobic growth on glucose, 14-fold upon aerobic growth on glucose and 33-fold upon aerobic growth at the expense of D-lactate.
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  • 5
    ISSN: 1432-072X
    Keywords: Redox control ; Enterobacteriaceae ; Anaerobiosis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Mutants of Escherichia coli were isolated in which transcription of the structural genes for hydrogenase (hyd) and for one of the components of formate dehydrogenase (fdh) (of the formate hydrogen-lyase complex) is coupled with that of the lacZ gene. They were — together with lac fusions of the nifH and nifL genes from Klebsiella — used to study regulation by redox control, of the expression of the respective structural genes. The following results were obtained: (i) β-galactosidase synthesis was fully repressed in the presence of O2 or nitrate (anaerobically), and induced in the absence of an external electron acceptor. Fumarate as terminal electron acceptor only marginally affected nif expression and partially repressed hyd and fdh expression. Redox control of the synthesis of hydrogenase and formate dehydrogenase, therefore, (as well as that of nif) acts at the level of transcription; the size of the redox potential seems to be correlated with the amount of repression; (ii) β-galactosidase synthesis in the hyd:: lac and fdh::lac fusion strains is induced by formate. At high concentrations formate reverses the repression by nitrate and fumarate but not that by oxygen.
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  • 6
    ISSN: 1525-1314
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Geosciences
    Notes: The South Karakorum margin, east of the Himalayan syntaxis, consist of an E–W elongated zone of young (10–3 Ma) high-grade metamorphic rocks (M2) and related migmatitic domes. This late tectono-metamorphic event post-dates the Palaeogene (55–37 Ma) phase of thickening of the belt featured by NW–SE structures and associated M1 amphibolite facies metamorphism (0.7 GPa, 700 °C). This M2 metamorphism is characterised by low-pressure, high-temperature conditions coeval with migmatite formation in response to a thermal increase of c. 150 °C compared to M1, culminating at a temperature of c. 770 °C and a pressure of 0.5–0.6 GPa. Rapid exhumation of migmatitic domes, at a rate of 5 mm yr−1, was accommodated by vertical extrusion, in the core of E–W crustal-scale folds. These crustal-scale folds formed in response to N–S syn-collisional shortening and were enhanced by thermal weakening of the migmatised continental crust.M2 metamorphism is spatially and temporarily associated with granitoids showing a mantle affinity, firmly suggesting that this could be the advective heat source for the granite and syenite generation and the subsequent migmatisation of the mid-crustal level. Such relationships between a mantle-related magmatism and a high-temperature metamorphism in a convergent shortening context are suggestive of the breakoff of the subducted Indian slab since 20 Ma.
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  • 7
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of metamorphic geology 7 (1989), S. 0 
    ISSN: 1525-1314
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Geosciences
    Notes: All along the Himalayan chain an axis of crystalline rocks has been preserved, made of the Higher Himalaya crystalline and the crystalline nappes of the Lesser Himalaya. The salient points of the metamorphism, as deduced from data collected in central Himalaya (central Nepal and Kumaun), are:〈list xml:id="l1" style="custom"〉1The Higher Himalaya crystalline, also called the Tibetan Slab, displays a polymetamorphic history with a first stage of Barrovian type overprinted by a lower pressure and/or higher temperature type metamorphism. The metamorphism is due to quick and quasi-adiabatic uplift of the Tibetan Slab by transport along an MCT ramp, accompanied by thermal refraction effects in the contact zone between the gneisses and their sedimentary cover. The resulting metamorphic pattern is an apparent (diachronic) inverse zonation, with the sillimanite zone above the kyanite zone.2Conversely, the famous inverted zonation of the Lesser Himalaya is basically a primary pattern, acquired during a one-stage prograde metamorphism. Its origin must be related to the thrusting along the MCT, with heat supplied from the overlying hot Tibetan Slab, as shown by synmetamorphic microstructures and the close geometrical relationships between the metamorphic isograds and the thrust.3Thermal equilibrium is reached between units above and below the MCT. Far behind the thrust tip there is good agreement between the maximum temperature attained in the hanging wall and the temperature of the Tibetan Slab during the second metamorphic stage; but closer to the MCT front, the thermal accordance between both sides of the thrust is due to a retrogressive metamorphic episode in the basal part of the Tibetan Slab.
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  • 8
    Electronic Resource
    Electronic Resource
    Amsterdam : Elsevier
    Earth and Planetary Science Letters 118 (1993), S. 263-279 
    ISSN: 0012-821X
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Geosciences , Physics
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  • 9
    Electronic Resource
    Electronic Resource
    Amsterdam : Elsevier
    Earth and Planetary Science Letters 126 (1994), S. 217-234 
    ISSN: 0012-821X
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Geosciences , Physics
    Type of Medium: Electronic Resource
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  • 10
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary In Escherichia coli K12, eight substrate-specific, membrane-bound enzymes II of the PEP-dependent carbohydrate: phosphotransferase system (PTS), specific for hexoses, hexosamines and hexitols, have been characterised in a series of isogenic and constitutive strains. In such mutants, lacking all but one enzyme II, the transport and vectorial phosphorylation activities as well as the chemotactical response in capillary tube assays have been compared. According to the data obtained, all enzymes II not only are directly involved in the transport and vectorial phosphorylation of their substrates, but they have also a primary role as the chemoreceptors for these substrates: (1) Metabolism of the attractant beyond the phosphorylation step is not a pre-requisite to eliciting positive chemotaxis. (2) Mutants, having only one enzyme II react in the capillary tube assay only to substrates of this enzyme II, but not to substrates of the missing enzymes II. This holds for enzymes II consisting of one membrane-bound protein as well as for systems containing a soluble factor III (FIII). (3) The substrate specificities or affinities, whether tested by transport and chemotaxis assays in vivo or by phosphorylation tests in vitro, are in correpondence. (4) The activities of enzymes II, regulated in a complex way at the level of enzyme synthesis and activity and tested as above, are also in agreement. (5) Mutants lacking the soluble proteins enzyme I or HPr of the PTS no longer respond chemotactically to any substrate taken up and phosphorylated by enzymes II. It is concluded that in PTS enzymes II some functions required for transport and chemotaxis are identical. It is suggested furthermore, that the alternation of intrinsic membrane-bound proteins between a phosphorylated and a dephosphorylated state, rather than binding of the substrate to the enzyme II, is the decisive stimulus in the chemotaxis toward carbohydrates taken up by these transport systems.
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