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High Specific Activity Iodination of -Globulin with Iodine-131 Monochloride^*

( Department of Radiation Biology, University of Rochester School of Medicine and Dentistry, Rochester, N.Y.)

A technic, efficient in use of I¹³¹, has been developed for introducing I¹³¹ into 4-mg. amounts of antibody or -globulin protein at a level of 10 mc, I¹³¹ per mg. protein with a resulting iodine content of 2–3 atoms per protein molecule of 160,000 molecular weight. Oak Ridge I¹³¹ was adjusted to pH 8 with borate buffer and the requisite amount of hydrochloric acid. To this solution was added Na₂SO₃ to destroy H₂O₂ produced by I¹³¹ β-radiation. Excess sulfite was oxidized by aerating the solution in a boiling water bath. On the addition of iodine monochloride to the cooled solution, I¹³¹C1 (or HOI¹³¹) was produced by exchange, and following the rapid addition of this solution to protein, also in pH 8 buffer, coupling of approximately 60 per cent of the I¹³¹ to protein occurred. When 10 mc. or less of Oak Ridge I¹³¹ was used, the addition of Na₂SO₃ and the aeration could be omitted, and a yield of about 60 per cent of I¹³¹ attached to protein was still obtained.

^* This paper is based on work performed under contract with the U.S. Atomic Energy Commission at the University of Rochester Atomic Energy Project, Rochester, New York.

Received 5/13/60.