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Principles of antibody elution
Author(s) -
Howard P.L.
Publication year - 1981
Publication title -
transfusion
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.045
H-Index - 132
eISSN - 1537-2995
pISSN - 0041-1132
DOI - 10.1046/j.1537-2995.1981.21582040807.x
Subject(s) - elution , van der waals force , hydrogen bond , ionic bonding , chemistry , antibody , ionic strength , hydrophobic effect , antigen , chromatography , biophysics , molecule , organic chemistry , immunology , ion , aqueous solution , biology
Antibody‐antigen binding depends upon ionic, hydrophobic, and hydrogen bonds, as well as van der Waals forces and three‐dimensional conformation. Antibody elution techniques attempt to break those forces by alterations of ionic strength, pH, thermal agitation, and the use of organic solvents. Because of the heterogeneity of the physical forces involved in binding, no single elution technique finds universal applicability to the disruption of all types of antibody‐antigen bonds.