ALBERT

All Library Books, journals and Electronic Records Telegrafenberg

X
feed icon rss

Your email was sent successfully. Check your inbox.

An error occurred while sending the email. Please try again.

Proceed reservation?

Export
Filter
Collection
Keywords
Publisher
Years
  • 1
    Electronic Resource
    Electronic Resource
    A mutant of Escherichia coli K12 deficient in the 5′–3′ exonucleolytic activity of DNA polymerase I (1973)
    Springer
    Molecular genetics and genomics 124 (1973), S. 83-96 
    Details
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The enzymatic properties of purified DNA polymerase I from a strain of Escherichia coli K12 with a mutation in the polA gene have been studied. The polymerizing activity of the mutant enzyme is similar to that of the enzyme from isogenic wild-type cells, when the activity is measured on exonuclease III treated calf-thymus DNA. Also the 3′–5′ exonucleolytic activity is not significantly different for both enzyme preparations. The 5′–3′ exonucleolytic activity of DNA polymerase I isolated from the mutant strain, however, is much lower than that of wild-type DNA polymerase I. The products formed by the action of the wild-type and the mutant enzyme on nicked circular double-stranded DNA of phage ϕX174′ (RFII DNA) were analysed by sucrose-gradient sedimentation and electron-microscopy. When RFII DNA was incubated with wild-type enzyme 80% of the molecules were converted into linear molecules. All linear molecules were shorter than one phage genome. Only 25% of the molecules were branched. After incubation of RFII DNA with the mutant enzyme 62% of the molecules have become linear. More than 90% of these linear molecules were branched and the majority of them was longer than one phage genome.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00267167
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 2
    Electronic Resource
    Electronic Resource
    Mechanism of formation of bacteriophage ϕX174 circular and catenated dimer RF+ DNA (1973)
    Springer
    Molecular genetics and genomics 126 (1973), S. 37-51 
    Details
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Pulse-chase and density shift experiments were performed with ϕX174 infected cells. For density shift experiments the cells were first incubated in [14C]thymine containing medium, and after filtration and washing, transferred into [3H]BrdUrd containing medium. Samples were taken at different times and replicative form (RF) component I DNA was isolated, which subsequently was separated in monomers and dimers by buoyant density and velocity gradient centrifugation. During the chase period, or during growth in heavy medium a small but significant decrease in label was observed in the original fully light dimer RF DNA fraction. A relative enrichment of label was found in the heavy-light dimer fraction after the density shift. By electron microscopy it was demonstrated that both circular and catenated dimers add to this increase. The implications of the results on the mechanism of formation of catenated and circular dimers and on the mechanism of ϕX174 recombination are discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00333480
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 3
    Electronic Resource
    Electronic Resource
    Preferential adsorption of high density lipoprotein (HDL) in blood plasma/polymer interaction (1985)
    New York : Wiley-Blackwell
    Die Makromolekulare Chemie 9 (1985), S. 99-102 
    Details
    ISSN: 0025-116X
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Physics
    Notes: A few studies on the adsorption of plasma proteins to polymeric surfaces show that major plasma proteins: albumin (Alb), fibrinogen (Fb) and immunoglobulin (IgG) are adsorbed in much smaller quantities from plasma than from protein solutions (1,2). Present results show that this difference in adsorption is due to the preferential adsorption of high density lipoprotein from plasma onto the material surfaces studied (PVC and PS).
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/macp.1985.020091985112
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 4
    Electronic Resource
    Electronic Resource
    Specific removal of low density lipoprotein from blood plasma (1985)
    New York : Wiley-Blackwell
    Die Makromolekulare Chemie 9 (1985), S. 151-154 
    Details
    ISSN: 0025-116X
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Physics
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/macp.1985.020091985120
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...