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Trypsin-resistant regions of thyroglobulin: possible relationship with intermonomeric contact site(s).

Upon incubation of bovine thyroglobulin with trypsin at high enzyme/substrate ratio, some fragments with apparent masses between 18 and 31 kDa resisted prolonged digestion. Their NH2-terminal sequences were determined. All fragments overlapped with some of the Cys-rich repeats that compose a large part of thyroglobulin and are predicted to have a rigid structure. Among the inserts that interrupt the cysteine-rich repeats, for which several data indicate a location at the surface of thyroglobulin, the insert of repeat 1.7 was unique because of its resistance to proteolysis. This insert, although exposed at the surface of the protein, may be hidden in a region of contact between thyroglobulin monomers.