X-Message-Number: 11933
Date: Thu, 10 Jun 1999 05:11:28 -0700 (PDT)
From: Doug Skrecky <>
Subject: cations and organic solute cryoprotection

  Hazen KC.  Bourgeois LD.  Carpenter JF.
  Department of Microbiology, University of Southwestern Louisiana, Lafayette
  Cryoprotection of antibody by organic
  solutes and organic solute/divalent cation mixtures.
  Archives of Biochemistry & Biophysics.  267(1):363-71, 1988 Nov 15.
  Antibodies are globular glycoproteins that protect animals from microbial and
  toxic insult. These proteins have proven to have substantial commercial and
  research value but are variably susceptible to freeze-thaw damage, thus
  limiting their usefulness. Several carbohydrates and divalent cations were
  examined alone and in combination to determine whether they could protect
  antibody from freeze-thaw damage. The amino acid proline was
  also tested. Two antibodies, derived from different sources and specific for
  different antigens, were tested by a direct enzyme-linked immunosorbent assay
  (ELISA). Confirmation of antibody freeze-lability was
  obtained by rocket electrophoresis and radial immunodiffusion tests. Neither
  carbohydrate nor divalent cation alone fully protected
  antibody activity from freeze-thaw damage. However, several
  combinations protected antibody activity completely when
  compared to their effect on antibody maintained at room
  temperature. In the case of affinity-purified antibody, full
  protection of antibody activity relative to an untreated
  control was obtained. In several instances, cryoprotection
  of antibody by solute-divalent cation combinations was
  synergistic and not an additive effect of each component. Alkaline
  phosphatase, an enzyme typically linked to antibody for an
  ELISA, was not freeze-thaw labile. These results indicate that
  antibody function can be fully protected from damage due to
  freeze-thaw treatment by organic solutes in combination with divalent

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