SPLITTING OF HUMAN THYROGLOBULIN .4. ANTIGENICITY OF PEPSIN-DERIVED FRAGMENTS

  • 1 January 1977
    • journal article
    • research article
    • Vol. 27  (2) , 245-253
Abstract
Purified human thyroglobulin (Tg) was hydrolyzed by pepsin. After completion of hydrolysis the pepsin hydrolyzate 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 2 fragments had sedimentation coefficients of 1.0 and 0.6, respectively. These fragments retained antigenic determinants reactive with 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.