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mods:
  schema location: http://www.loc.gov/mods/v3 http://www.loc.gov/standards/mods/v3/mods-3-2.xsd
  title info:
    non sort: The
    title: biosynthesis, structure, and in vitro interaction of human decorin using the vaccinia virus/T7 bacteriophage system
  title info:
    title: Biosynthesis, structure, and in vitro interaction of human decorin using the vaccinia virus/T seven bacteriophage system
  name:
    name part: Krishnan, Priya
    name part: 1967-
    role:
      role term: creator
  type of resource: text
  genre: bibliography
  origin info:
    place:
      place term: xx
    date issued: 1997
    issuance: monographic
  language:
    language term: eng
  physical description:
    form: print
    extent: xii, 147 leaves : illustrations ; 28 cm.
  abstract: Decorin is a small chondroitin sulfate proteoglycan found
  abstract: ubiquitously in tissues. The biological function of decorin
  abstract: is not well understood, although several studies have
  abstract: suggested a role in regulating the deposition of the collagen
  abstract: network, stabilizing the tissue architecture and modulating
  abstract: cellular metabolism. Many of the biological assays used to
  abstract: study the role of decorin and its interactions with other
  abstract: matrix molecules, have used proteoglycans extracted from
  abstract: tissues using denaturing solvents such as urea and guanidine
  abstract: hydrochloride. These reagents may have irreversible effects
  abstract: on protein structure, which could alter the binding potential
  abstract: of proteoglycans with other matrix molecules. This study has
  abstract: utilized the vaccinia virus/T7 bacteriophage expression
  abstract: system to overexpress decorin glycoforms. Overexpression
  abstract: resulted in secretion and purification under native
  abstract: conditions of 30 mg decorin/109 cells per day. The decorin
  abstract: protein expressed, comprised of subpopulations of
  abstract: differentially glycosylated forms of the protein. Far LTV
  abstract: circular dichroism spectra of native decorin showed a minimum
  abstract: at 218 nm, consistent with a secondary structure that is
  abstract: predominantly B-sheet. Circular dichroism spectra of
  abstract: recombinant decorin purified in chaotropic solvents and
  abstract: tissue extracted decorin revealed a minimum of 205 nm
  abstract: indicating a loss of secondary structure. In vitro binding
  abstract: studies on recombinant decorin purified under native and
  abstract: denaturing conditons with collagenous proteins suggested
  abstract: there are structure dependent and independent domains that
  abstract: mediate these interactions. A biophysical analysis of the
  abstract: changes on the secondary conformation of decorin and a
  abstract: structurally related proteoglycan, biglycan, suggest these
  abstract: urea, and are unable to refold to their original conformation
  abstract: upon the removal of urea. These data confirm the importance
  abstract: of secondary structure to the function of decorin.
  note: by Priya Krishnan.
  note: Vita.
  note: "Major Subject: Biochemistry".
  note: In title, numerals are used.
  note: Issued also on microfiche from University Microfilms Inc.
  note: Includes bibliographical references: pages 132-145.
  note: Ph. D. Texas A&M University 1997.
  subject:
    topic: Major biochemistry
  identifier: 98-00762 UMI
  identifier: http://proxy.library.tamu.edu/login
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    location:
      url: http://proxy.library.tamu.edu/login
  record info:
    record content source: TXA
    record creation date: 980406
    record change date: 20190325093501.0
    record identifier: in00001415025