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  • 1
    Electronic Resource
    Electronic Resource
    The cps gene cluster of Salmonella strain LT2 includes a second mannose pathway: sequence of two genes and relationship to genes in the rfb gene cluster (1991)
    Springer
    Molecular genetics and genomics 227 (1991), S. 173-180 
    Details
    ISSN: 1617-4623
    Keywords: GC ratio ; cps ; rfb ; Phosphomannomutase ; Mannose-1-phosphate guanyltransferase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary We report the presence in Salmonella enterica strain LT2 (serovar thyphimurium) of duplicate genes for two steps in the synthesis of GDP-mannose. The previously known genes, rfbK (phosphomannomutase) and rfbM (mannose-l-phosphate guanyltransferase), are part of the gene cluster for the O antigen. The two new genes, cpsB and cpsG, respectively, are thought to be part of the gene cluster for the M antigen capsular polysaccharide, present in many Enterobacteriaceae. The two genes have been sequenced and have a GC content of 0.61, suggesting an origin outside of Salmonella. Comparison of the inferred protein sequences for cpsB and rfbM shows 57% identity of amino acids whereas for cpsG and rfbK there is only 19% identity. It is suggested that the greater divergence between cpsG and rfbK may be due to a period of accelerated evolution, perhaps precipitated by transfer of the genes from another species.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00259668
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  • 2
    Electronic Resource
    Electronic Resource
    A Novel Technique for the Effective Production of Short Peptide Analogs from Concatameric Short Peptide Multimers (2000)
    Springer
    Molecules and cells 10 (2000), S. 236-240 
    Details
    ISSN: 0219-1032
    Keywords: Cleavable Linker Peptide ; Concatameric Peptide Multimers ; Peptide Analogs ; Tandemly Repeated DNA Cassette
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract We designed a basic unit of the modified chicken gonadotropin releasing hormone II (cGnRH-II) peptide containing a trypsin cleavable linker peptide at both ends of the original peptide. We made a synthetic DNA coding for the modified cGnRH-II peptide with asymmetric and complementary cohesive ends of linker nucleotides. A tandemly repeated DNA cassette for the expression of concatameric short peptide multimers was constructed by ligating the basic units. The expressed peptide multimers were purified and subject to amino-terminal sequence analysis, which displayed the amino acid sequences expected from the designed nucleotides of the expression cassette. The monomeric cGnRH-II peptide analogs were generated after trypsin digestion. The present results showed that the technique developed for the production of the concatameric peptide multimers with cleavable linker peptides can be generally applicable to the production of short peptide analogs.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s10059-000-0236-9
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