PMID: 3758078Sep 15, 1986Paper

Structural differences around hormonogenic sites on thyroglobulins from different species detected by monoclonal antibodies

European Journal of Biochemistry
C T ChanR L Himsworth

Abstract

Thyroxine remains attached to its synthetic site in thyroglobulin until it is released by proteolysis. Strong homology in the primary sequence surrounding thyroxine-forming residues in thyroglobulins from various species suggests a unique three-dimensional structure at hormonogenic sites. To examine this, two thyroxine-binding mouse anti-(chicken thyroglobulin) monoclonal antibodies, 1A10 and 5F6, were used as probes for this region in an enzyme-linked immunosorbent inhibition assay. The thyroxine content of thyroglobulins had a marked positive influence on the monoclonal antibody binding: when the thyroxine content of human thyroglobulin rose by 6.6-fold, cross-reactivities rose 25-fold for the 1A10 monoclonal antibody and 17.6-fold for the 5F6 monoclonal antibody. However, interspecies comparison of thyroglobulin preparations with similar thyroxine content showed lower than expected cross-reactivities for human, pig and sheep thyroglobulins when compared with chicken thyroglobulin. Only when the thyroxine content of heterologous thyroglobulin preparations was two or three times higher did the cross-reactivities equal or surpass that of chicken thyroglobulin. It is concluded that in thyroglobulin there are structural differenc...Continue Reading

References

Apr 20, 1973·Biochimica Et Biophysica Acta·M RollandS Lissitzky
Dec 1, 1982·The Biochemical Journal·P G ByfieldR L Himsworth
Jan 30, 1984·Biochemical and Biophysical Research Communications·A B RawitchJ W Hamilton
Apr 15, 1984·The Biochemical Journal·P G ByfieldR L Himsworth
Jul 1, 1981·Clinical Endocrinology·C J PearceR L Himsworth
Oct 1, 1980·European Journal of Biochemistry·C MarriqS Lissitzky

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