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  • Flavoprotein  (2)
  • Petrocoptis  (2)
  • tectonic block  (2)
  • Springer  (6)
  • 2005-2009
  • 1990-1994  (6)
  • 1975-1979
  • 1
    Electronic Resource
    Electronic Resource
    Isolation and characterization of two new N-glycosidase type-1 ribosome-inactivating proteins, unrelated in amino-acid sequence, fromPetrocoptis species (1994)
    Springer
    Planta 194 (1994), S. 487-491 
    Details
    ISSN: 1432-2048
    Keywords: Petrocoptis ; Petroglaucin ; Petrograndin ; Ribosome-inactivating protein ; rRNA N-glycosidase ; Translation (inhibition)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Two new N-glycosidase type-1 ribosome-inactivating proteins (RIPs), denoted petroglaucin 1 and petrograndin, respectively, were isolated from the plantsPetrocoptis glaucifolia (Lag.) Boiss sp.viscosa (Rothm.) Laínz andPetrocoptis grandiflora Rothm. These new RIPs do not share H2N-terminal amino-acid sequence homology with petroglaucin (now denoted as petroglaucin 2), the only other type-1 RIP to be isolated fromP. glaucifolia (Arias et al. (1992) Planta186, 532–540). Petroglaucin 1 shares amino-acid sequence homology with RIPs from Cucurbitaceae while petroglaucin 2 and petrograndin do so with saporins and dianthin 30 (Caryophyllaceae). The new RIPs strongly inhibited protein synthesis at subnanomolar concentrations in rabbit reticulocyte lysates and other eukaryotic cell-free systems, but they were inactive on bacterial ribosomes.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00714460
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  • 2
    Electronic Resource
    Electronic Resource
    Purification and characterization of anl-amino-acid oxidase fromChlamydomonas reinhardtii (1992)
    Springer
    Planta 188 (1992), S. 13-18 
    Details
    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
    URL: http://dx.doi.org/10.1007/BF01160707
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  • 3
    Electronic Resource
    Electronic Resource
    Isolation and partial characterization of a new ribosome-inactivating protein from Petrocoptis glaucifolia (Lag.) Boiss (1992)
    Springer
    Planta 186 (1992), S. 532-540 
    Details
    ISSN: 1432-2048
    Keywords: Petrocoptis ; Protein synthesis inhibitor ; Ribosome inactivating protein ; Translation (inhibition)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Petrocoptis glaucifolia, a paleoendemic member of the Caryophyllaceae from the North of Spain, was found to contain at least five proteins that inhibit protein synthesis in a rabbit reticulocyte lysate. One of them, for which the name petroglaucin is proposed, was purified to apparent electrophoretic homogeneity by chromatography through S-Sepharose Fast Flow, Sephadex G-75 and CM-Sepharose Fast Flow. The apparent Mr of the preparation was 27500. This protein does not contain appreciable glycan chains and displays 45.8% of NH2-terminal amino-acid sequence homology with some ribosome-inactivating proteins from Saponaria officinalis, another member of the Caryophyllaceae. Petroglaucin shows the following functional properties: (i) it strongly inhibits the rabbit-reticulocyte-lysate system and Vicia sativa cell-free extracts, both coded by endogenous messengers, and also inhibits poly(U)-directed polyphenylalanine synthesis by Vicia sativa cell-free extracts and purified rat-liver ribosomes; (ii) it shows much less inhibitory capacity in wheat-germ, Cucumis sativus and rat-liver cell-free systems coded by endogenous messengers; (iii) the inhibitory effects on purified rat-liver ribosomes were irreversible; (vi) it promotes the release of adenine from purified rat-liver ribosomes. The total activity of this translational inhibitor has been found to increase up to 11-fold during its purification, indicating that some regulatory factor that normally blocks the translational inhibitory activity of the ribosome-inactivating protein in crude extracts of the plant is removed during purification.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00198033
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  • 4
    Electronic Resource
    Electronic Resource
    Purification and characterization of an l-amino-acid oxidase from Chlamydomonas reinhardtii (1992)
    Springer
    Planta 188 (1992), S. 13-18 
    Details
    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
    URL: http://dx.doi.org/10.1007/BF00198934
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  • 5
    Electronic Resource
    Electronic Resource
    Some aspects of the seismic hazard in Panama City (1990)
    Springer
    Natural hazards 3 (1990), S. 233-248 
    Details
    ISSN: 1573-0840
    Keywords: Seismic hazard ; seismicity ; tectonic block ; seismic hazard prediction ; earthquake catalogue ; completeness and homogeneity
    Source: Springer Online Journal Archives 1860-2000
    Topics: Energy, Environment Protection, Nuclear Power Engineering , Geography , Geosciences
    Notes: Abstract The definition of earthquake sources in the Panama region on the basis of both tectonics and average seismicity rates, have recently led to the concept of a microplate surrounded by seismically active areas. The effects of these earthquakes on the place where the most important concentration of investments and population is located, the capital city of Panama, are analyzed in this paper using statistical approaches. The parameters of Gumbel's Type-I distribution of extreme values for a continuous interval of 60 yr annual maximum magnitudes were used to make probabilistic estimations of the seismic hazard in Panama City. An earthquake with magnitude 7.5 is capable of producing a modified Mercalli intensity VII in Panama City, provided the source distance is of the order of 100 km. This earthquake has a probability of occurrence of 69% in 50 yr.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00124579
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  • 6
    Electronic Resource
    Electronic Resource
    Probabilistic seismic hazard maps for Panama (1991)
    Springer
    Natural hazards 4 (1991), S. 1-6 
    Details
    ISSN: 1573-0840
    Keywords: Seismic hazard zonation ; probabilistic iso-intensity maps ; tectonic block ; seismic sources ; seismic hazard computation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Energy, Environment Protection, Nuclear Power Engineering , Geography , Geosciences
    Notes: Abstract Probabilistic seismic hazard maps in term of Modified Mercalli (MM) intensity are derived by applying the ‘Cornell-McGuire’ method to four earthquake source zones in Panama and adjacent areas. The maps contain estimates of the maximum MM intensity for return periods of 5, 25 and 100 yr. The earthquake phenomenon is based on the point source model. The probabilistic iso-intensity map for a return period of 50 yr indicates that the Panama Suture Zone (PSZ) could experience a maximum (MM) intensity IX, and the Panama Fracture Zone (PFZ) an MM intensity VIII, for the rest of the area this varies from IV up to VIII. The present study intends to serve as a reference for more advanced approaches, to stimulate discussions and suggestions on the data base, assumptions and inputs, and path for the risk based assessment of the seismic hazard in the site selection and in the design of common buildings and engineering.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00126555
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