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Splitting of human thyroglobulin. IV. The antigenicity of the pepsin-derived fragments
Purified human thyroglobulin (Tg) was hydrolysed by pepsin. After completion of hydrolysis the pepsin hydrolysate was passed through a Sephadex G-200 column to remove undigested Tg. Further isolation of the enzymatic fragments was effected by passage through a Sephadex G-75 column. Two discrete fragments, termed pep I and pep II, were separated. The two fragments had sedimentation coefficients of 1-0 and 0-6, respectively. These fragments retained antigenic determinants reactive with both hetero-and auto-antibodies to Tg. The larger fragment, pep I, possessed all antigenic determinants to intact Tg while pep II lacked some determinants. Neither fragment contained novel determinants resulting from proteolytic degradation.
Purified human thyroglobulin (Tg) was hydrolysed by pepsin. After completion of hydrolysis the pepsin hydrolysate was passed through a Sephadex G-200 column to remove undigested Tg. Further isolation of the enzymatic fragments was effected by passage through a Sephadex G-75 column. Two discrete fragments, termed pep I and pep II, were separated. The two fragments had sedimentation coefficients of 1-0 and 0-6, respectively. These fragments retained antigenic determinants reactive with both hetero-and auto-antibodies to Tg. The larger fragment, pep I, possessed all antigenic determinants to intact Tg while pep II lacked some determinants. Neither fragment contained novel determinants resulting from proteolytic degradation.