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  • 1995-1999  (2)
  • Affinity chromatography  (1)
  • Block downdating  (1)
  • 1
    Electronic Resource
    Electronic Resource
    Perturbation and error analyses for block downdating of a Cholesky decomposition (1996)
    Springer
    BIT 36 (1996), S. 247-263 
    Details
    ISSN: 1572-9125
    Keywords: Block downdating ; Cholesky decomposition ; condition number ; error analysis ; perturbation theory ; seminormal equations
    Source: Springer Online Journal Archives 1860-2000
    Topics: Mathematics
    Notes: Abstract A new perturbation result is presented for the problem of block downdating a Cholesky decompositionX T X = R T R. Then, a condition number for block downdating is proposed and compared to other downdating condition numbers presented in literature recently. This new condition number is shown to give a tighter bound in many cases. Using the perturbation theory, an error analysis is presented for the block downdating algorithms based on the LINPACK downdating algorithm and stabilized hyperbolic transformations. An error analysis is also given for block downdating using Corrected Seminormal Equations (CSNE), and it is shown that for ill-conditioned downdates this method gives more accurate results than the algorithms based on the LINPACK downdating algorithm or hyperbolic transformations. We classify the problems for which the CSNE downdating method produces a downdated upper triangular matrix which is comparable in accuracy to the upper triangular factor obtained from the QR decomposition by Householder transformations on the data matrix with the row block deleted.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01731982
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    NADH oxidase ofThermus thermophilus HB8 overproduced fromEscherichia coli (1995)
    Springer
    Protoplasma 184 (1995), S. 104-110 
    Details
    ISSN: 1615-6102
    Keywords: NADH oxidase ; Thermostable flavoprotein ; Affinity chromatography ; Codon usage
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary An NADH oxidase purified from the extreme thermophileThermus thermophilus HB8 is a monomeric flavoprotein with a 1 ∶ 1 ratio of flavin-adenine dinucleotide (FAD) to the polypeptide chain. It catalyzes in vitro the oxidation of reduced NADH or NADPH with the formation of H2O2. The gene encoding the NADH oxidase fromT. thermophilus HB8 was cloned, and its nucleotide sequence was determined. The molecular mass of 22,749 Da, as deduced from thenox gene, agrees with that of the purified NADH oxidase fromT. thermophilus HB8, as estimated by mass spectrometry. Thenox gene does not contain a GX4GK consensus sequence typical for nucleotide binding proteins. Thenox gene was overexpressed inEscherichia coli, and a protocol for the rapid purification of theE. coli-borneT. thermophilus NADH oxidase or its His6-tagged analogue was developed by using thermal denaturation step and affinity chromatography.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01276906
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    Paper (German National Licenses)
    Fulltext
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