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  • 1985-1989  (3)
  • 1
    Electronic Resource
    Electronic Resource
    Introduction of the transposon Tn919 into Lactobacillus curvatus Lc2-c (1989)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 65 (1989), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract The conjugative transposon Tn919 was introduced into the plasmid cured strain Lactobacillus curvatus Lc 2-c by means of filter mating. Enterococcus faecalis GF590 was used as donor. The transfer frequency was 2 × 10−7/recipient. Random insertion was proved by Southern hybridization. Segregation after 10 passages without selective pressure could not be detected. The transposition site remained unchanged and no subsequent second-site transposition occured.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1989.tb03604.x
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    ld-Carboxypeptidase activity in Escherichia coli (1986)
    Springer
    Archives of microbiology 144 (1986), S. 175-180 
    Details
    ISSN: 1432-072X
    Keywords: d-Amino acids ; ld-carboxypeptidase ; Escherichia coli ; Ether treated cells ; Thienamycin
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The activities of the ld-carboxypeptidases of Escherichia coli K12 and of a mutant strain 155 with reduced activities were studied with the aid of ether treated cells. Evidence was obtained that was consistent with the suggestion that in both strains two ld-carboxypeptidase activities are present. Activity I degrades the nucleotide activated precursor UDP-MurNAc-tetrapeptide and activity II splits off d-alanine residues from position 4 of the peptide subunits in the nascent murein. In the mutant strain activity I is reduced 10fold compared with strain K 12, whereas activity II is not affected. The two activities could be distinguished with regard to their sensitivity to d-amino acids and the β-lactam antibiotic thienamycin.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00414731
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    ld-Carboxypeptidase activity in Escherichia coli (1986)
    Springer
    Archives of microbiology 144 (1986), S. 181-186 
    Details
    ISSN: 1432-072X
    Keywords: Antibiotics ; d-Amino acids ; ld-Carboxypeptidase ; Escherichia coli ; Murein synthesis ; Nocardicin A
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A ld-carboxypeptidase from Escherichia coli K 12 was isolated by Tris-EDTA treatment and purified to electrophoretic homogeneity by DEAE-cellulose chromatography. The enzyme has a molecular weight of approximately 12,000 as determined by sodium dodecyl sulfatepolyacrylamide electrophoresis and by Sephadex G-100 gel filtration. The studies of the substrate specificity of the enzyme revealed that UDP-MurNAc-tetrapeptide is a superior substrate, with a K m value of 1×10-4 mol/l. The activity of the ld-carboxypeptidase was inhibited by d-amino acids and the β-lactam antibiotic nocardicin A. K i values of 0.3 and 43 mmol/l were determined for nocardicin A and d-homoserine, respectively. The properties of the purified enzyme correspond to activity I in ether treated cells.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00414732
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    Paper (German National Licenses)
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