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Evidence for a preferential iodination site within the thyroglobulin molecule
1Third Department of Internal Medicine, University of Yamanashi Medical School, Japan.
Mouse 330 kDa thyroglobulin labeled in vivo was analyzed using a tryptic peptide mapping technique and high performance liquid chromatography (HPLC). 30 min after Na125I injection, one peptide spot (spot 7) on a silica gel plate was the only prominent labeled peptide, followed by other labeled peptide spots after 1 h. HPLC showed that spot 7 was rich in monoiodotyrosine. The ratios between the iodoamino acids were strictly maintained from 1 to 6 h after Na125I injection. Spot 7 was again the first spot that appeared from the samples of iodine-deficient mice. These data indicate that there is some preferential iodination site(s) within the thyroglobulin molecule and also that their iodoamino acid composition is predetermined.
Mouse 330 kDa thyroglobulin labeled in vivo was analyzed using a tryptic peptide mapping technique and high performance liquid chromatography (HPLC). 30 min after Na125I injection, one peptide spot (spot 7) on a silica gel plate was the only prominent labeled peptide, followed by other labeled peptide spots after 1 h. HPLC showed that spot 7 was rich in monoiodotyrosine. The ratios between the iodoamino acids were strictly maintained from 1 to 6 h after Na125I injection. Spot 7 was again the first spot that appeared from the samples of iodine-deficient mice. These data indicate that there is some preferential iodination site(s) within the thyroglobulin molecule and also that their iodoamino acid composition is predetermined.