Splitting of human thyroglobulin. IV. The antigenicity of the pepsin derived fragments

W. A. Stylos, N. R. Rose

Research output: Contribution to journalArticlepeer-review

Abstract

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 9.6, 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.

Original languageEnglish (US)
Pages (from-to)245-253
Number of pages9
JournalClinical and Experimental Immunology
Volume27
Issue number2
StatePublished - 1977

ASJC Scopus subject areas

  • Immunology and Allergy
  • Immunology

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