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  • 1
    Electronic Resource
    Electronic Resource
    Comparison of metabolic activation of carcinogens in human, rat, and hamster hepatocytes
    Amsterdam : Elsevier
    Mutation Research/Environmental Mutagenesis and Related Subjects 182 (1987), S. 31-39 
    Details
    ISSN: 0165-1161
    Keywords: (Hamster) Aflatoxin B"1 ; (Human) ; (Rat) ; Acetylaminofluorene ; Aminofluorene ; Carcinogens ; Hepatocytes ; metabolic activation
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Medicine
    Type of Medium: Electronic Resource
    URL: http://linkinghub.elsevier.com/retrieve/pii/0165-1161(87)90005-7
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  • 2
    Electronic Resource
    Electronic Resource
    Initial characterization of autoprocessing and active-center mutants of CMV proteinase (1996)
    Springer
    The protein journal 15 (1996), S. 763-774 
    Details
    ISSN: 1573-4943
    Keywords: Cytomegalovirus proteinase ; CMV ; calorimetry ; ultracentrifugation ; mutant
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract Human cytomegalovirus (CMV) encodes a unique serine proteinase that is required in the maturation of the viral capsid. The CMV proteinase can undergo autocatalytic activation and is subject to proteolytic self-inactivation. Mutant enzyme forms were prepared to eliminate the initial autoprocessing site and thus form an active single-chain protein for structure-function studies. Two mutants of CMV proteinase were cloned and expressed inEscherichia coli. The A143V mutant was a conservative substitution at the first internal cleavage site. The S132A mutant modified one of the triad of residues responsible for catalytic activity. Through the use of computer-controlled high-cell-density fermentations the mutant proteins were expressed inE. coli at ∼170mg/L as both soluble (∼40% of total) and inclusion-body forms (∼60% of total). The soluble enzyme was purified by standard methods; inclusion-body protein was isolated by standard methods after refolding and solubilization in guanidine or urea. Sedimentation equilibrium and sedimentation velocity analyses reveal that the enzyme undergoes concentration-dependent aggregation. It exhibits a monomer⇔dimer equilibrium (K d =1ΜM) at low concentrations and remains dimeric at high concentrations (28 mg/ml). Differential scanning calorimetry data for protein thermal unfolding fit best to a non-two-state model with two components (T m =52.3 and 55.3
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01887151
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    Paper (German National Licenses)
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