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  • exponential decay  (3)
  • Flavoprotein  (2)
  • Immunohistochemistry  (2)
  • Springer  (7)
  • 1
    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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  • 2
    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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  • 3
    Electronic Resource
    Electronic Resource
    The Transmission Problem of Viscoelastic Waves (2000)
    Springer
    Acta applicandae mathematicae 62 (2000), S. 1-21 
    Details
    ISSN: 1572-9036
    Keywords: transmission problem ; exponential decay ; partially viscoelastic ; materials with memory
    Source: Springer Online Journal Archives 1860-2000
    Topics: Mathematics
    Notes: Abstract In this paper we consider the transmission problem of viscoelastic waves. That is, we study the wave propagations over materials consisting of elastic and viscoelastic components. We show that for this types of materials the dissipation produced by the viscoelastic part is strong enough to produce exponential decay of the solution, no matter how small is its size. We also show that the linear model is well posed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1006449032100
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  • 4
    Electronic Resource
    Electronic Resource
    Uniform Rates of Decay in Anisotropic Thermo-Viscoelasticity (1998)
    Springer
    Acta applicandae mathematicae 50 (1998), S. 207-224 
    Details
    ISSN: 1572-9036
    Keywords: viscoelasticity ; exponential decay ; initial boundary-value problems
    Source: Springer Online Journal Archives 1860-2000
    Topics: Mathematics
    Notes: Abstract We consider the anisotropic and inhomogeneous thermo-viscoelastic equation. We prove that the first and second-order energy decay exponentially as time goes to infinity provided the relaxation function also decays exponentially to zero. While if the relaxation functions decay polynomially to zero, then the energy decays also polynomially. That is, the kernel of the convolution defines the rate of decay of the solution.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1005830811242
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  • 5
    Electronic Resource
    Electronic Resource
    Decay rates for viscoelastic plates with memory (1996)
    Springer
    Journal of elasticity 44 (1996), S. 61-87 
    Details
    ISSN: 1573-2681
    Keywords: 35B40 ; 35L05 ; 35L70 ; viscoelasticity ; exponential decay ; initial boundary value problems
    Source: Springer Online Journal Archives 1860-2000
    Topics: Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics , Physics
    Notes: Abstract We consider the viscoelastic plate equation and we prove that the first and second order energies associated with its solution decay exponentially provided the kernel of the convolution also decays exponentially. When the kernel decays polynomially then the energy also decays polynomially. More precisely if the kernel g satisfies g(t) ⩽ -c0g(t)1+1/p and g,g1+1/p ∈ L1(ℝ) with p 〉 2, then the energy decays as 1/(1+t)p.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00042192
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  • 6
    Electronic Resource
    Electronic Resource
    Tachykinin-like immunoreactivity in the sinus venosus of the dogfish (Scyliorhinus canicula) (1994)
    Springer
    Cell & tissue research 278 (1994), S. 171-175 
    Details
    ISSN: 1432-0878
    Keywords: Tachykinin ; Substance P ; Sinus venosus ; Heart ; Immunohistochemistry ; Dogfish, Scyliorhinus canicula (Elasmobranchii)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract The sinus venosus of the elasmobranch heart is characterized by the presence of large bundles of unmyelinated nerve fibres that bulge into the cardiac lumen, below the endocardium. In the dogfish (Scyliorhinus canicula), these fibres contain numerous dense-core membrane-bounded granules of about 200 nm in diameter. Most intramural ganglion cells of the sinus venosus also show densely packed granules similar to those found in the subendocardial fibres. We have observed strong substance-P-like immunoreactivity in the large fibre bundles and in the perikarya of the ganglion cells. Preabsorption of the antisera with fragment 7–11 of substance P has shown that the antisera recognize the tachykinin canonic sequence. Our findings suggest that an undetermined tachykinin is secreted in the elasmobranch heart, and that it is probably released into the blood stream in the context of a little-known neuroendocrine system.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00305789
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  • 7
    Electronic Resource
    Electronic Resource
    Tachykinin-like immunoreactivity in the sinus venosus of the dogfish (Scyliorhinus canicula) (1994)
    Springer
    Cell & tissue research 278 (1994), S. 171-175 
    Details
    ISSN: 1432-0878
    Keywords: Key words: Tachykinin ; Substance P ; Sinus venosus ; Heart ; Immunohistochemistry ; Dogfish ; Scyliorhinus canicula (Elasmobranchii)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract. The sinus venosus of the elasmobranch heart is characterized by the presence of large bundles of unmyelinated nerve fibres that bulge into the cardiac lumen, below the endocardium. In the dogfish (Scyliorhinus canicula), these fibres contain numerous dense-core membrane-bounded granules of about 200 nm in diameter. Most intramural ganglion cells of the sinus venosus also show densely packed granules similar to those found in the subendocardial fibres. We have observed strong substance-P-like immunoreactivity in the large fibre bundles and in the perikarya of the ganglion cells. Preabsorption of the antisera with fragment 7–11 of substance P has shown that the antisera recognize the tachykinin canonic sequence. Our findings suggest that an undetermined tachykinin is secreted in the elasmobranch heart, and that it is probably released into the blood stream in the context of a little-known neuroendocrine system.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00305789
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