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Binding of ^99mTc Ion to Hemoglobin

New England Medical Center, Tufts University School of Medicine, Boston, Massachusetts

Correspondence: For reprints contact: Mrinal K. Dewanjee, Dept. of Radiology, Div. of Nuclear Medicine, Proger 4, Tufts-New England Medical Center Hospitals, Boston, Mass. 02111.

ABSTRACT

The mechanism and preferential site of binding of ^99mTc ion to hemoglobin had been determined by the separation of ^99mTc-hemoglobin from ^99mTc-citrate and ^99mTc-pertechnetate ion with a Sephadex G25 column. This purified fraction was analyzed by the HCl/acetone mixture to determine the ^99mTc activity distribution with heme and globin. Most of the ^99mTc activity is associated with globin fraction. The preferred chain for ^99mTc ion binding was determined by the splitting of ^99mTc-hemoglobin with parachloromercuribenzoate solution followed by separation with a diethylaminoethyl cellulose column equilibrated with phosphate buffer. The ^99mTc ion, like Cr³⁺ ion, tends to bind preferentially with the beta chain of hemoglobin.

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