Thermodynamic basis for the abnormal solubility of monoclonal cryoimmunoglobulins

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...

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Bibliographic Details
Published in:The Journal of biological chemistry 1980-07, Vol.255 (14), p.6532-6534
Main Authors: Middaugh, C R, Lawson, E Q, Litman, G W, Tisel, W A, Mood, D A, Rosenberg, A
Format: Article
Language:English
Subjects:
Animals
Cattle
Cryoglobulins
Fructose-Bisphosphate Aldolase
Hemoglobin A
Hemoglobin, Sickle
Humans
Immunoglobulin G
Immunoglobulin M
Oxyhemoglobins
Polyethylene Glycols
Rabbits
Serum Albumin, Bovine
Solubility
Thermodynamics
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Summary: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.
ISSN:0021-9258
1083-351X
DOI:10.1016/S0021-9258(18)43596-X