Bovine thyrotropin radiolabeled stoichiometrically with chloramine T was subjected to high pressure liquid chromatography on a Waters' Protein I-125 column. More than 80% of the radioactivity eluted after the Na125I ('salt') peak. In contrast, thyrotropin bioactivity eluted before the salt peak. Radiolabeled thyrotropin affinity-purified with thyroid plasma membranes eluted after the salt peak. Discordance between the thyrotropin bioactivity and radioactivity elution profiles was confirmed by labeling thyrotropin with 125I by lactoperoxidase and then measuring both bioactivity and radioactivity in each chromatographic fraction. These data suggest that the bioactivity in radiolabeled thyrotropin may not be inherent in the radiolabeled molecules.
Studies on the bioactivity of radiolabeled, highly-purified bovine thyrotropin / N. A., Takai; Filetti, Sebastiano; B., Rapoport. - In: BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS. - ISSN 0006-291X. - STAMPA. - 97:2(1980), pp. 566-573.
Studies on the bioactivity of radiolabeled, highly-purified bovine thyrotropin
FILETTI, SEBASTIANO;
1980
Abstract
Bovine thyrotropin radiolabeled stoichiometrically with chloramine T was subjected to high pressure liquid chromatography on a Waters' Protein I-125 column. More than 80% of the radioactivity eluted after the Na125I ('salt') peak. In contrast, thyrotropin bioactivity eluted before the salt peak. Radiolabeled thyrotropin affinity-purified with thyroid plasma membranes eluted after the salt peak. Discordance between the thyrotropin bioactivity and radioactivity elution profiles was confirmed by labeling thyrotropin with 125I by lactoperoxidase and then measuring both bioactivity and radioactivity in each chromatographic fraction. These data suggest that the bioactivity in radiolabeled thyrotropin may not be inherent in the radiolabeled molecules.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.