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
  • 1
    Electronic Resource
    Electronic Resource
    Production, crystallization and diffraction to atomic resolution of an antibody Fv specific for the blood-group A oligosaccharide antigen (1998)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 54 (1998), S. 1456-1459 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: The histoblood-group ABO carbohydrate antigens are well known as important factors in blood transfusions, but they can also act as receptors for infectious agents and have been implicated in susceptibility to certain carcinomas. A single-chain variable-domain antigen-binding fragment (scFv) gene based on the known sequence of an anti-blood-group-A monoclonal antibody (AC1001) has been synthesized and expressed in Escherichia coli. The purified scFv preparation existed primarily in the monomeric form but also contained large amounts of dimeric and higher oligomeric forms. The corresponding variable-domain antigen-binding fragment (Fv) was generated by cleaving the VL–VH linker with subtilisin, and its activity was demonstrated by surface plasmon resonance with an immobilized bovine serum albumin A–trisaccharide conjugate (KD = 290 µM). AC1001 Fv crystals grown in the presence of N-acetylgalactosamine diffracted to 0.93 Å resolution. This is the first reported example of a crystal of an antibody antigen-binding fragment diffracting to atomic resolution.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444998005824
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 2
    facet.materialart.
    Unknown
    Dolomite dissolution: An alternative diagenetic pathway for the formation of palygorskite clay (2019)
    Wiley
    Details
    Publication Date: 2019
    Description: Abstract Palygorskite is a fibrous, magnesium‐bearing clay mineral commonly associated with Late Mesozoic and Early Cenozoic dolomites. The presence of palygorskite is thought to be indicative of warm, alkaline fluids rich in Si, Al and Mg. Palygorskite has been interpreted to form in peritidal diagenetic environments, either as a replacement of detrital smectite clay during a dissolution–precipitation reaction or solid‐state transformation, or as a direct precipitate from solution. Despite a lack of evidence, most diagenetic studies involving these two minerals posit that dolomite and palygorskite form concurrently. Here, petrological evidence is presented from the Umm er Radhuma Formation (Palaeocene–Eocene) in the subsurface of central Qatar for an alternative pathway for palygorskite formation. The Umm er Radhuma is comprised of dolomitized subtidal to peritidal carbonate cycles that are commonly capped by centimetre‐scale beds rich in palygorskite. Thin section, scanning electron microscopy and elemental analyses demonstrate that palygorskite fibres formed on both the outermost surfaces of dissolved euhedral dolomite crystals and within partially to completely dissolved dolomite crystal cores. These observations suggest that dolomite and palygorskite formed sequentially, and support a model by which the release of Mg2+ ions and the buffering of solution pH during dolomite dissolution promote the formation of palygorskite. This new diagenetic model explains the co‐occurrence of palygorskite and dolomite in the rock record, and provides valuable insight into the specific diagenetic conditions under which these minerals may form.
    Print ISSN: 0037-0746
    Electronic ISSN: 1365-3091
    Topics: Geosciences
    Published by Wiley
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    PAPER CURRENT
  • 3
    facet.materialart.
    Unknown
    Production, crystallization and diffraction to atomic resolution of an antibody Fv specific for the blood-group A oligosaccharide antigen (1998)
    International Union of Crystallography
    Details
    Publication Date: 1998-11-01
    Description: The histoblood-group ABO carbohydrate antigens are well known as important factors in blood transfusions, but they can also act as receptors for infectious agents and have been implicated in susceptibility to certain carcinomas. A single-chain variable-domain antigen-binding fragment (scFv) gene based on the known sequence of an anti-blood-group-A monoclonal antibody (AC1001) has been synthesized and expressed in Escherichia coli. The purified scFv preparation existed primarily in the monomeric form but also contained large amounts of dimeric and higher oligomeric forms. The corresponding variable-domain antigen-binding fragment (Fv) was generated by cleaving the VL–VH linker with subtilisin, and its activity was demonstrated by surface plasmon resonance with an immobilized bovine serum albumin A–trisaccharide conjugate (KD = 290 µM). AC1001 Fv crystals grown in the presence of N-acetylgalactosamine diffracted to 0.93 Å resolution. This is the first reported example of a crystal of an antibody antigen-binding fragment diffracting to atomic resolution.
    Print ISSN: 0907-4449
    Electronic ISSN: 1399-0047
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Published by International Union of Crystallography
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    PAPER CURRENT
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...