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  • 1
    Electronic Resource
    Electronic Resource
    Proteolysis in the obligate methylotroph Methylophilus methylotrophus (1987)
    Springer
    Archives of microbiology 147 (1987), S. 394-398 
    Details
    ISSN: 1432-072X
    Keywords: Obligate methylotroph ; Methylophilus methylotrophus ; Proteolysis ; Abnormal protein ; Interferon α-2 ; Respiratory inhibition
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract This report represents the first demonstration of degradation of intracellular protein in the obligate methylotroph, Methylophilus methylotrophus. Proteolysis in batch culture was followed by a pulse-chase protocol which included chloramphenicol during the chase period to prevent re-incorporation of the radio-label, l-[4,5-3H] isoleucine. Starvation for a nitrogen source mildly stimulated proteolysis whereas starvation for the carbon source (0.5% v/v methanol) inhibited proteolysis by over 50%. Respiratory inhibitors (e.g. 2,4-DNP) caused a rapid decline in both intracellular ATP concentration and protein catabolism. Proteins synthesized after the addition of methanol (5% v/v) and ethanol (5% v/v) to the growth medium were subject to rapid degradation. Breakdown of abnormal proteins generated by treatment with dihydrostreptomycin and puromycin was also inhibited by inhibitors of respiration and deprivation of carbon source. The stability of an heterologous gene product, interferon α-2, was also investigated; loss of immunoreactivity was reduced in the absence of methanol but not prevented.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00406139
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Protein turnover in a psychrotrophic bacterium (1985)
    Springer
    Archives of microbiology 142 (1985), S. 28-33 
    Details
    ISSN: 1432-072X
    Keywords: Arthrobacter ; Psychrophile ; Psychrotroph ; Protein turnover temperature effects on protein stability
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Protein breakdown in pulse-labelled and longlabelled cells of Arthrobacter S 1-55, a psychrotrophic bacterium, has been assessed at different temperatures. The temperature at which the cells were grown and labelled affected the breakdown of pulsed-labelled but not long-labelled proteins. Inhibitors of ATP synthesis inhibited proteolysis. Miscoding antibiotics stimulated the production of rapidly degradable proteins.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00409232
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    A possible new role for the anti-ageing peptide carnosine (2000)
    Springer
    Cellular and molecular life sciences 57 (2000), S. 747-753 
    Details
    ISSN: 1420-9071
    Keywords: Key words. Protein; aging; ageing; carbonyl; glycation; proteolysis; lipofuscin; advanced glycosylation end-product.
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract. The naturally occurring dipeptide carnosine (β-alanyl-L-histidine) is found in surprisingly large amounts in long-lived tissues and can delay ageing in cultured human fibroblasts. Carnosine has been regarded largely as an anti-oxidant and free radical scavenger. More recently, an anti-glycating potential has been discovered whereby carnosine can react with low-molecular-weight compounds that bear carbonyl groups (aldehydes and ketones). Carbonyl groups, arising mostly from the attack of reactive oxygen species and ow-molecular-weight aldehydes and ketones, accumulate on proteins during ageing. Here we propose, with supporting evidence, that carnosine can react with protein carbonyl groups to produce protein-carbonyl-carnosine adducts (‘carnosinylated’ proteins). The various possible cellular fates of the carnosinylated proteins are discussed. These proposals may help explain anti-ageing actions of carnosine and its presence in non-mitotic cells of long-lived mammals.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s000180050039
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    Paper (German National Licenses)
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