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  • Chlamydomonas (l-amino-acid oxidase)  (2)
  • Petrocoptis  (2)
  • (Vitis vinifera x Vitis rupestris) x Vitis riparia  (1)
  • Springer  (5)
  • 2005-2009
  • 1990-1994  (5)
  • 1975-1979
Collection
Keywords
Publisher
  • Springer  (5)
Years
  • 2005-2009
  • 1990-1994  (5)
  • 1975-1979
Year
  • 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
    Levels of 4-hydroxystilbene-oxidizing isoperoxidases related to constitutive disease resistance in in vitro-cultured grapevine (1992)
    Springer
    Plant cell, tissue and organ culture 29 (1992), S. 63-70 
    Details
    ISSN: 1573-5044
    Keywords: axillary bud culture ; cell culture ; peroxidase isoenzymes ; viniferin synthesis ; Vitis vinifera ; (Vitis vinifera x Vitis rupestris) x Vitis riparia
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A zymographic screening of peroxidases (EC 1.11.1.7) capable of oxidizing 4-hydroxystilbene was carried out by means of the peroxidase-catalyzed oxidative coupling of 4-hydroxystilbene and 4-aminoantipyrine. This screening reveals that only a few isoperoxidases are active in oxidizing 4-hydroxystilbene to viniferin-type compounds in in vitro cultures of grapevine. Unlike total peroxidase activity measured with 4-methoxy-α-naphthol, the levels of total peroxidase activity measured using 4-hydroxystilbene are related to disease resistance against downy mildew in axillary bud cultures of Vitis vinifera and (Vitis vinifera x Vitis rupestris) x Vitis riparia. From this observation, and using the above zymographic assay, it was found that a 4-hydroxystilbene-oxidizing isoperoxidase was overexpressed in both leaves and stems of the hybrid in relation to the increase in disease resistance of this species. These results suggest that constitutive 4-hydroxystilbene-oxidizing isoperoxidases may participate through their role in viniferin synthesis in the constitutive resistance mechanism that grapevines show against downy mildew.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00033609
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