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The origin of the electrophoretic doublet of thyroglobulin.

Biochem Biophys Res Commun

August 1992

Centro di Endocrinologia e Oncologia Sperimentale del C.N.R., University of Naples 2nd Medical School, Italy.

Bovine and human thyroglobulin show two closely migrating bands in reducing SDS-PAGE. Limited digestion with chymotrypsin, trypsin and thermolysin converted the slower band of the doublet into a peptide identical to the faster band, with an apparent mass of 270 kDa, in both species. The starting point of the faster band of the doublet was established at Ileu 520 with native bovine Tg and at Ser 503 with native human Tg, and at Ser 503 and Ser 504 with chymotrypsin-digested bovine and human Tg, respectively.

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