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  • 1
    Electronic Resource
    Electronic Resource
    Involvement of mercury methylation in microbial mercury detoxication (1982)
    Springer
    Archives of microbiology 131 (1982), S. 176-177 
    Details
    ISSN: 1432-072X
    Keywords: Methylation of mercury ; Detoxication of mercury ; Mercury sensitivity ; Vitamin B12 auxotroph ; Methylcobalamin ; Clostridium cochlearium
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A vitamin B12 requiring strain was isolated fromChlostridium cochlearium T-2 C which is known to synthesize various types of vitamin B12 including methylcobalamin and has an ability to methylate inorganic mercury. The vitamin B12 auxotroph lacking the mercury-methylating activity showed higher sensitivity to inorganic mercury than its original strain, while the sensitivity of both strains to methylmercury was relatively low and essentially the same. These data seem to present affirmative evidence to postulate the physiological role of methylcobalamin-dependent methylation of mercury to be a process of detoxication.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01054003
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  • 2
    Electronic Resource
    Electronic Resource
    Possible role of membrane proteins in mercury resistance of Enterobacter aerogenes (1981)
    Springer
    Archives of microbiology 130 (1981), S. 93-95 
    Details
    ISSN: 1432-072X
    Keywords: Membrane proteins ; Mercury resistance ; Plasmid-mediated ; Uptake of mercury ; Permeability ; Outer membrane ; Enterobacter aerogenes
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Mercury resistance shown by a strain of Enterobacter aerogenes was found to be determined by a plasmid. The resistance appeared to be not due to enzymatic volatilization of mercury, but due to the alteration in cellular permeability to mercury. Comparison of the outer membrane proteins was made between the resistant cells and the sensitive counterparts obtained by the treatment with mitomycin C, showing that two proteins with molecular weight of 46,000 and 44,000 had disappeared from the outer membrane along with the plasmid by the curing. These results suggest that the two membrane proteins mediating the cellular permeability to mercury compound may be responsible for the mercury resistance of the strain.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00411057
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    Paper (German National Licenses)
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