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Thermodynamic basis for the abnormal solubility of monoclonal cryoimmunoglobulins.

Authors
  • Middaugh, C R
  • Lawson, E Q
  • Litman, G W
  • Tisel, W A
  • Mood, D A
  • Rosenberg, A
Type
Published Article
Journal
The Journal of biological chemistry
Publication Date
Jul 25, 1980
Volume
255
Issue
14
Pages
6532–6534
Identifiers
PMID: 7190147
Source
Medline
License
Unknown

Abstract

The thermodynamics of both normal and abnormal (disease-associated) protein solubility has been examined. It is shown that the atypical behavior of monoclonal cryoimmunoglobulins can be explained by the formation of one or a few additional electrostatic contacts or, less frequently, a larger number of van der Waals interactions in the protein-rich solid phase relative to normal immunoglobulin. It is hypothesized that cryoimmunoglobulins represent the outer edge of the solubility distribution of total serum immunoglobulin.

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