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  • Galois cohomology  (2)
  • Medicago (root nodules, N2 fixation)  (2)
  • Springer  (4)
  • American Physical Society
  • Blackwell Publishing Ltd
Collection
Publisher
  • Springer  (4)
  • American Physical Society
  • Blackwell Publishing Ltd
Years
  • 1
    Electronic Resource
    Electronic Resource
    Springer
    K-Theory 5 (1991), S. 555-566 
    ISSN: 1573-0514
    Keywords: Characteristic classes ; multiplicative transfer ; Galois cohomology
    Source: Springer Online Journal Archives 1860-2000
    Topics: Mathematics
    Notes: Abstract Let F be a field, G F its absolute Galois group, ρ: G F→GLπ(C) a continuous complex representation of G F and c i(ρ)∈ H2i(F, Z) its Chern classes. We show, under a mild assumption on F. that c i (ρ)=0 for all i⩾2. For general F, one has that 2ci (ρ)=0 for all i⩾ 2.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    K-Theory 7 (1993), S. 55-100 
    ISSN: 1573-0514
    Keywords: K 2 ; Galois cohomology ; descent ; number fields
    Source: Springer Online Journal Archives 1860-2000
    Topics: Mathematics
    Description / Table of Contents: Abstract LetF be a field andE/F be a Galois extension with groupG. In this paper, we establish canonical isomorphisms: $$\begin{gathered} Ker(K_2 (F) \to K_2 (E)^G ) \cong H^1 (G,K_3 (E_0 )_{ind} ); \hfill \\ Coker(K_2 (F) \to K_2 (E)^G ) \cong H^2 (G,K_3 (E_0 )_{ind} ), \hfill \\ \end{gathered} $$ whereE 0 is the field of constants ofE andK 3(E 0)ind is the indecomposable quotient ofK 3(E 0). We exploit these isomorphisms in various situations: general fields, function fields of varieties, number fields.
    Notes: Résumé SoientF un corps commutatif etE/F une extension galoisienne de groupeG. Le but de cet article est d'établir et d'exploiter dans diverses situations des isomorphismes canoniques: $$\begin{gathered} Ker(K_2 (F) \to K_2 (E)^G ) \cong H^1 (G,K_3 (E_0 )_{ind} ); \hfill \\ Coker(K_2 (F) \to K_2 (E)^G ) \cong H^2 (G,K_3 (E_0 )_{ind} ), \hfill \\ \end{gathered} $$ oùE 0 est le corps des constantes deE etK 3(E 0)ind est le quotient indécomposable deK 3(E 0).
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 1432-2048
    Keywords: Aspartate aminotransferase (immunocytochemistry, subcellular fractionation) ; Glutamate oxaloacetic transaminase ; Medicago (root nodules, N2 fixation) ; Nitrogen fixation ; Root nodule
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Aspartate aminotransferase (AAT; EC 2.6.1.1) catalyzes the synthesis of the amino acid aspartate which, in alfalfa root nodules, serves as the immediate precursor of the primary N-transport compound, asparagine. The enzyme AAT may also be important in providing substrates for host-plant and bacteroid respiration. The enzyme occurs as two isoenzymes, AAT-1 and AAT-2, with AAT-1 more abundant in roots and AAT-2 predominant in root nodules. To further elucidate the role of AAT in root-nodule metabolism, subcellular fractionation and immunocytochemical methods were used to determine the intra- and intercellular localization of these two isozymes. Fractionation of nodule subcellular components showed that AAT-2 was localized in amyloplasts. Immunogold labelling with AAT-2 antibodies unequivocally confirmed this, showing that AAT-2 was localized in nodule amyloplasts and leaf chloroplasts. In root nodules, the density of immunogold labelling of infected cell plastids was almost four times that of uninfected cell plastids. The data suggest that aspartate biosynthesis in alfalfa root nodules occurs primarily in the plastids of infected cells.
    Type of Medium: Electronic Resource
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  • 4
    ISSN: 1432-2048
    Keywords: Aspartate aminotransferase (immunocytochemistry, subcellular fractionation) ; Glutamate oxaloacetic transaminase ; Medicago (root nodules, N2 fixation) ; Nitrogen fixation ; Root nodule
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Aspartate aminotransferase (AAT; EC 2.6.1.1) catalyzes the synthesis of the amino acid aspartate which, in alfalfa root nodules, serves as the immediate precursor of the primary N-transport compound, asparagine. The enzyme AAT may also be important in providing substrates for host-plant and bacteroid respiration. The enzyme occurs as two isoenzymes, AAT-1 and AAT-2, with AAT-1 more abundant in roots and AAT-2 predominant in root nodules. To further elucidate the role of AAT in root-nodule metabolism, subcellular fractionation and immunocytochemical methods were used to determine the intra- and intercellular localization of these two isozymes. Fractionation of nodule subcellular components showed that AAT-2 was localized in amyloplasts. Immunogold labelling with AAT-2 antibodies unequivocally confirmed this, showing that AAT-2 was localized in nodule amyloplasts and leaf chloroplasts. In root nodules, the density of immunogold labelling of infected cell plastids was almost four times that of uninfected cell plastids. The data suggest that aspartate biosynthesis in alfalfa root nodules occurs primarily in the plastids of infected cells.
    Type of Medium: Electronic Resource
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