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Influence of radioiodination on the adsorption of IgG and serum albumin to polystyrene

Journal Article · · Anal. Biochem.; (United States)
The adsorption of radioiodinated rabbit IgG and bovine serum albumin (BSA) to polystyrene tubes was investigated. Adsorption isotherms where the proportion of the protein bound was relatively constant over a range of intermediate protein concentrations, and where the proportion bound was protein dependent, were obtained. To investigate the effects of radioiodination, proteins labelled to give a wide range of substitution ratios (0.03 to 3.7 /sup 125/I/ protein molecule) were employed. While labeling did not appear to affect BSA adsorption, the kinetics of IgG binding were altered in a number of ways. The proportion bound in the concentration independent region was decreased even at substitution ratios less than or equal to 0.2. In addition, while all preparations of iodinated BSA, and IgG preparations with less than or equal to 1.6 /sup 125/I/IgG, gave bimodal adsorption isotherms, with more heavily labeled IgG (less than or equal to 2.5 /sup 125/I/IgG) the apparent high affinity binding to the plastic surface was abolished. These results indicate that radioiodination substantially alters the kinetics of the binding of IgG to polystyrene. In addition, the results obtained are discussed with respect to previous relevant and often apparently contradictory findings.
Research Organization:
Univ. College, Galway, Ireland
OSTI ID:
5871100
Journal Information:
Anal. Biochem.; (United States), Journal Name: Anal. Biochem.; (United States) Vol. 158:2; ISSN ANBCA
Country of Publication:
United States
Language:
English