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  • 1
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Industrial & engineering chemistry research 28 (1989), S. 1873-1878 
    ISSN: 1520-5045
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology , Process Engineering, Biotechnology, Nutrition Technology
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Industrial & engineering chemistry research 28 (1989), S. 1879-1883 
    ISSN: 1520-5045
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology , Process Engineering, Biotechnology, Nutrition Technology
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Plant, cell & environment 12 (1989), S. 0 
    ISSN: 1365-3040
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract. Under stress conditions (darkness, nitrogen starvation, high ammonium concentrations, glutamine synthetase and glutamate synthase inhibition) glutamate dehydrogenase animating activity levels of Chlamydomonas cells varied inversely to those of glutamine synthetase. Nitrogen and carbon sources also influenced glutamate dehydrogenase levels in Chlamydomonas, the highest values being found in cells cultured mixotrophically with ammonium, under which conditions glutamate dehydrogenase and glutamine synthetase levels were likewise inversely related. These facts, together with the analysis of internal fluctuations of ammonium, 2-oxoglutarate, and the amino acid pool as well as the variations of certain enzymes involved in carbon metabolism indicate that glutamate dehydrogenase animating activity is adaptative, being involved in the maintenance of intracellular levels of L-glutamate when they cannot be maintained by the GS-GOGAT cycle, and probably more connected with carbon than nitrogen metabolism.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Physiologia plantarum 84 (1992), S. 0 
    ISSN: 1399-3054
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Interaction between induction of carbonic anhydrase (CA) activity, induction of inorganic carbon (Ci) concentrating mechanisms and the photorespiratory glycolate pathway has been studied in wild type 6145c and photorespiratory mutant 18–7F (low in phosphoglycolate phosphatase activity) cells of C. reinhardtii. Cell transfer from high CO2 (5%, v/v) to low CO2 (0.03%) provoked an increase of extracellular and total (extracellular plus intracellular) CA in both wild type and mutant cells. During adaptation to low CO2 conditions, both strains excreted ammonium to the medium at a similar rate in the presence of l-methionine-d-l-sulfoximine (MSX), an inhibitor of glutamine synthetase (GS). MSX also provoked ammonium excretion by air adapted wild type and mutant cells, even though both strains had high levels of CA activity and of Ci concentrating activities.GS increased in both strains after transfer from high to low CO2 conditions. However, this increase was abolished by aminooxyacetate, an inhibitor of the glyoxylate-serine aminotransferase, and by glycolaldehyde, an inhibitor of triose phosphate to ribulose 1,5-bisphosphate conversion. CA synthesis did not occur in the presence of either aminooxyacetate or glycolaldehyde. Algae grown in high CO2 in the presence of aminooxyacetate did not induce Ci concentrating mechanisms. Integration of these three processes, i.e., CA synthesis, Ci-concentration, and photorespiratory glycolate pathway is proposed in the framework of carbon metabolism of the alga.
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  • 5
    ISSN: 1432-2048
    Keywords: l-amino-acid oxidase (molecular properties) ; Chlamydomonas (l-amino-acid oxidase) ; Flavoprotein
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Anl-amino-acid oxidase (EC 1.4.3.1) that catalyzes the oxidative deamination of twelvel-amino acids has been purified 21-fold and with 14% yield to electrophoretic homogeneity fromChlamydomonas reinhardtii cells by ammonium-sulfate fractionation, gel filtration through Sephacryl and Superose, anion-exchange chromatography and preparative electrophoresis in polyacrylamide gels. The native enzyme is a protein of 470 kDa and consists of eight identical or similarsized subunits of 60 kDa each. Optimum pH and temperature were 8.2 and 55° C, respectively, with a Q10 (45–55° C) of 1.7 and an activation energy of 45 kJ · mol−1. Its absorption spectrum showed, in the visible region, maxima at 360 and 444 nm, characteristic of a flavoprotein with a calculated flavin content of 7.7 mol FAD per mol of native enzyme. ApparentK m values of the twelvel-amino acids which can act as substrates ofl-amino-acid oxidase ranged between 31 μM for phenylalanine and 176 μM for methionine. The effect of several specific group reagents, chelating agents and bivalent cations on enzyme activity has also been studied.
    Type of Medium: Electronic Resource
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  • 6
    ISSN: 1432-2048
    Keywords: l-amino-acid oxidase (molecular properties) ; Chlamydomonas (l-amino-acid oxidase) ; Flavoprotein
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract An l-amino-acid oxidase (EC 1.4.3.1) that catalyzes the oxidative deamination of twelve l-amino acids has been purified 21-fold and with 14% yield to electrophoretic homogeneity from Chlamydomonas reinhardtii cells by ammonium-sulfate fractionation, gel filtration through Sephacryl and Superose, anion-exchange chromatography and preparative electrophoresis in polyacrylamide gels. The native enzyme is a protein of 470 kDa and consists of eight identical or similarsized subunits of 60 kDa each. Optimum pH and temperature were 8.2 and 55° C, respectively, with a Q10 (45–55° C) of 1.7 and an activation energy of 45 kJ · mol−1. Its absorption spectrum showed, in the visible region, maxima at 360 and 444 nm, characteristic of a flavoprotein with a calculated flavin content of 7.7 mol FAD per mol of native enzyme. Apparent K m values of the twelve l-amino acids which can act as substrates of l-amino-acid oxidase ranged between 31 μM for phenylalanine and 176 μM for methionine. The effect of several specific group reagents, chelating agents and bivalent cations on enzyme activity has also been studied.
    Type of Medium: Electronic Resource
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  • 7
    ISSN: 1432-0827
    Keywords: Bone mass ; Seasonal bone changes ; Metacarpal morphometry ; Computed radiogrammetry ; Body weight ; Bone densitometry
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine , Physics
    Notes: Abstract We studied the behavior of radiogrammetric and densitometric measurements in relation to season and body weight in a group of 30 healthy premenopausal women. Measurements were made at 6-month intervals, in summer/fall when bone density increases and in winter/spring when bone density declines. Total body bone mineral content (TBBMC) and regional bone mineral content (RBMC) were measured using dual-energy X-ray absorptiometry (DXA). Metacarpal radiogrammetry was carried out with computed radiography. Weight and body mass index increased significantly in winter (P〈0.05) and total body and RBMC decreased (P〈0.001). The opposite occurred in summer: weight and body mass index decreased significantly (P〈0.05) and total body and regional bone mineral content increased (P〈0.001). Differences in TBBMC persisted when the measurement was corrected for weight (TBBMC/W) (P〈0.001), but not for metacarpal cortical thickness corrected for weight. In the first measurement made there were significant relations between weight and both TBBMC (P〈0.001) and metacarpal cortical thickness (P〈0.005). The relation between weight and TBBMC remained significant in later measurements, but the relation between weight and metacarpal cortical thickness ceased to be significant in the second and fourth measurements. Our results show that there is an important seasonal variation in bone mass and that DXA is more sensitive than radiogrammetry in registering these changes.
    Type of Medium: Electronic Resource
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  • 8
    ISSN: 1432-2048
    Keywords: L-amino acids (utilization) ; Chlamydomonas ; Deaminase (extracellular)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract When grown in the light and in a Tris-acetate phosphate medium, cells of Chlamydomonas reinhardtii Dang. can use the following l-amino acids as a sole nitrogen source: asparagine, glutamine, arginine, lysine, alanine, valine, leucine, isoleucine, serine, methionine, histidine, and phenylalanine, whereas, in the absence of acetate, the cells only used l-arginine. The utilization system in the acetate medium consisted of an extracellular deaminating activity induced by l-amino acids; it took between 10 to 30 h before the system appeared in cells previously grown with ammonium. This deaminase activity was nonspecific, required an organic carbon source for its de-novo synthesis, and was sensitive to high ammonium concentration and light deprivation.
    Type of Medium: Electronic Resource
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  • 9
    Electronic Resource
    Electronic Resource
    Springer
    Molecular genetics and genomics 209 (1987), S. 633-633 
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Type of Medium: Electronic Resource
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  • 10
    Electronic Resource
    Electronic Resource
    Chichester : Wiley-Blackwell
    Organic Magnetic Resonance 32 (1994), S. 321-325 
    ISSN: 0749-1581
    Keywords: neo-clerodane diterpenoids ; 2D NMR ; Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: High-field 2D NMR studies were performed on nine neo-clerodane diterpenoids. Unambiguous assignments of the 13C signals and proton chemical shifts were achieved which led to the revision of some previous assignments.
    Additional Material: 4 Tab.
    Type of Medium: Electronic Resource
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