Abstract
Large fractions of immunoglobulin G (IgG) from mammalian species show high affinities for protein A isolated from staphylococcus aureus. The radiochemical purity of 99mTc-labelled IgG was determined by means of protein A, covalently bound to sepharose, by a column radiochromatographic technique and by a simpler and more rapid technique in vials. Different labelling methods produced different radiochemical purities. Limitations and applications of the testing systems are discussed.
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