ヒト甲状腺腫瘍組織におけるチログロブリンの性状に関する研究

抄録

The nature of thyroglobulin which has been purified from human thyroid tumor tissue has been examined. The following findings were obtained.
The thyroglobulin content of tumor tissue was decreased markedly in cancer and the iodine content of thyroglobulin was also decreased in benign tumors and markedly decreased in cancer. However, there was no significant defference detected in amino acid composition among thyroglobulin preparations obtained from normal tissue, benign and cancer thyroid tissues. Concerning the carbohydrate content of thyroglobulin, sialic acid, which is probably located at the terminal position of the carbohydrate chains, was markedly decreased in cancer tissues. The hexose content varied among preparations. The affinity of thyroglobulin to lectins suggested that the structure of carbohydrate moiety on cancer thyroglobulin may be abnormal and various. The antigenic activity of tumor thyroglobulin varies greatly, suggesting heterogeneity of peptide moiety of thyroglobulin.