Affordable Access

Thermodynamic basis for the abnormal solubility of monoclonal cryoimmunoglobulins.

Authors
Type
Published Article
Journal
The Journal of biological chemistry
Publication Date
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.

Statistics

Seen <100 times