Abstract
SERUM albumins have been widely studied with respect to their ability to bind a wide range of substances1–3. Of particular interest are the nature of the binding sites and the question of whether the same sites are involved in binding different substances. Attempts have been made to elucidate the nature of the binding sites by determining the effect of chemical alteration of the serum albumin molecule on its binding properties3,4. Unfortunately direct chemical alteration does not permit evaluation of whether loss of binding is due to an alteration of the site itself or some non-specific alteration of the molecule elsewhere, resulting in either a subsequent disruption of the site or to a non-specific effect on the site.
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PRESSMAN, D., RADZIMSKI, G. Iodination of Specific Sites on Bovine Serum Albumin. Nature 186, 1049–1050 (1960). https://doi.org/10.1038/1861049a0
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DOI: https://doi.org/10.1038/1861049a0
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