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  schema location: http://www.loc.gov/mods/v3 http://www.loc.gov/standards/mods/v3/mods-3-2.xsd
  title info:
    title: Studies in enzymatic peptide synthesis
  name:
    name part: West, James Blair
    name part: 1957-
    role:
      role term: creator
  name:
    name part: Bergbreiter, David E.
    role:
      role term: degree committee member.
  name:
    name part: Meyer, Edgar F.
    role:
      role term: degree committee member.
  name:
    name part: Scott, A. Ian
    role:
      role term: degree committee member.
  name:
    name part: Wong, Chi-Huey
    role:
      role term: degree supervisor.
  name:
    name part: Texas A & M University
    role:
      role term: degree granting institution.
  type of resource: text
  genre: bibliography
  genre: Academic theses
  origin info:
    place:
      place term: xx
    date issued: 1988
    issuance: monographic
  language:
    language term: eng
  physical description:
    form: print
    extent: xii, 103 leaves : illustrations ; 29 cm
  abstract: Chapter I. The incorporation of D-amino acids into peptides via kinetic approach enzymatic peptide synthesis is examined. D-amino acid esters were found to be fairly efficient acyl-acceptors under conditions of high organic cosolvent. Various parameters effecting peptide yield are examined, such as nucleophile concentration# enzyme concentration# temperature, type and concentration of cosolvent, and enzyme immobilization. A novel type of amino-acid analog, a-nitro, a-methyl acids, is found to be a moderately efficient acyl-donor, with D-specificity. Chapter II. As a method for avoiding potential secondary hydrolysis of peptide products in protease-catalyzed peptide synthesis# various lipases lacking amidase activity are examined as catalysts in peptide synthesis. While synthesis does occur# reaction times are sluggish and it is found to be difficult to minimize hydrolysis of the acyl-donor ester. Chapter III. The chemical modification of proteases to esterases to achieve a peptide synthesis catalyst without amidase activity is examined. (His[95])N-methyl Chymotrypsin is synthesized and found to be very effective in peptide synthesis, while completely lacking the amidase activity. Chapter IV. Techniques are developed for determining nucleophile affinity in protease catalyzed peptide synthesis. This not only allows quantification of nucleophile specificity, which may be different from hydrolytic leaving group specificty, it allows for changes in active site architecture due to chemical or genetic alteration to be mapped.
  note: "Major subject: Chemistry."
  note: Typescript (photocopy).
  note: Vita.
  note: Ph. D. Texas A & M University 1988
  note: Includes bibliographical references.
  subject:
    topic: Amino acids
  subject:
    topic: Peptides
    topic: Synthesis
  subject:
    topic: Major chemistry
  identifier: http://proxy.library.tamu.edu/login
  identifier: https://hdl.handle.net/1969.1/DISSERTATIONS-1016984
  identifier: http://gateway.proquest.com/openurl
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    location:
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  related item:
    location:
      url: https://hdl.handle.net/1969.1/DISSERTATIONS-1016984
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      url: http://gateway.proquest.com/openurl
  record info:
    record content source: TXA
    record creation date: 900620
    record change date: 20220103134827.0
    record identifier: in00000896588
    language of cataloging:
      language term: eng