rdf-syntax-grammar
mods:
  schema location: http://www.loc.gov/mods/v3 http://www.loc.gov/standards/mods/v3/mods-3-2.xsd
  title info:
    title: pH-biased isoelectric trapping separations
  title info:
    title: PH biased isoelectric trapping separations
  name:
    name part: Shave, Evan Eric
    name part: 1976-
    role:
      role term: creator
  name:
    name part: Vigh, Gyula
    role:
      role term: thesis advisor.
  type of resource: text
  genre: bibliography
  origin info:
    place:
      place term: txu
    date issued: 2006
    issuance: monographic
  language:
    language term: eng
  physical description:
    form: electronic
    form: remote
  abstract: The classical isoelectric trapping (IET) technique, using the multicompartment electrolyzer (MCE), has been one of the most successful electrophoretic techniques in preparative-scale protein separations. IET is capable of achieving high resolution discrimination of proteins, by isolating proteins in between buffering membranes, in their isoelectric state. However, due to the inherent nature of the IET process, IET has suffered several shortcomings which have limited its applicability. During a classical IET separation, a protein gets closer and closer to its pI value, thus the charge of the protein gets closer and closer to zero. This increases the likelihood of protein precipitation and decreases the electrophoretic velocity of the protein, thus making the separation very long. Furthermore, the problems are aggravated by the fact that the instrumentation currently used for IET is not designed to maximize the efficiency of electrophoretic separations. To address these problems, a new approach to IET has been developed, pH-biased IET. By controlling the solution pH throughout the separation, such that it is not the same as the protein's pI values, the problems of reduced solubility and low electrophoretic migration velocity are alleviated. The pH control comes from a novel use of isoelectric buffers (also called auxiliary isoelectric agents or pH-biasers). The isoelectric buffers are added to the sample solution during IET and are chosen so that they maintain the pH at a value that is different from the pI value of the proteins of interest. Two new pieces of IET instrumentation have been developed, resulting in major improvements in protein separation rates and energy efficiency. A variety of separations, of both small molecules and proteins, have been successfully performed using the pH-biased IET principle together with the new instrumentation.
  note: by Evan Eric Shave.
  note: "Major Subject: Chemistry"
  note: Title from author supplied metadata (automated record created on Feb. 23, 2007.)
  note: Vita.
  note: Abstract.
  note: Electronic resource.
  note: Mode of access: World Wide Web.
  note: System requirements: World Wide Web access and Adobe Acrobat Reader.
  note: Ph. D. Texas A&M University 2005.
  note: Includes bibliographical references.
  note: Text (Dissertation).
  subject:
    topic: Major chemistry
  subject:
    topic: protein separations
  subject:
    topic: isoelectric trapping
  identifier: http://hdl.handle.net/1969.1/4184
  record info:
    record content source: TXA
    record creation date: 070326
    record change date: 20151104163209.0
    record identifier: in00002222439