Abstract

The iodine monochloride (ICl) technique is used to radiolabel proteins under mild experimental conditions. Proteins labeled by this technique have been shown to have both in vitro and in vivo characteristics often superior to those proteins labeled by the more frequently used chloramine-T method. Although first published more than two decades ago, use of the ICl technique has largely been superceded by other more recently developed iodination methods. This paper attempts to reintroduce the oxidative ICl method to the research community. This is accomplished by the presentation of a detailed protocol for a convenient modification of the original technique. A review of the qualities of the iodinated proteins produced by the ICl and other iodination methods is also discussed.

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