[Dissociation of thyroglobulin by tetraphenylborate ion].
Purified bovine and ovine thyroglobulins (19 S) are partially dissociated into 12-S subunits after treatment with sodium tetraphenyl borate. The extent of dissociation obtained by sodium tetraphenyl borate or sodium dodecyl sulfate treatment is the same. The electrophoretic mobilities on acrylamide gels of sodium tetraphenyl borate-resistant molecules and of native thyroglobulin are identical. Sodium dodecyl sulfate-resistant molecules move more slowly than the native protein.
Mauchamp
J
J
Laboratoire de Biochimie Générale et Comparée, Collège de France, Place Marcellín Berthelot, Paris 5e, France.
D000818:Animals; D002417:Cattle; D004591:Electrophoresis, Polyacrylamide Gel; D007202:Indicators and Reagents; D012756:Sheep; D013775:Tetraphenylborate; D013954:Thyroglobulin / Q000737:chemistry* / Q000302:isolation & purification
D007202:Indicators and Reagents; D013775:Tetraphenylborate; D013954:Thyroglobulin