Abstract
Samples of the colloid in rat thyroid follicles were obtained by micropuncture of superficial follicles in the isthmus in vivo and of superficial and deeper follicles in saline perfused thyroids. The protein composition of the samples was analyzed by microgel electrophoresis on polyacrylamide gels at neutral pH. The protein separation patterns were recorded by microdensitometry after staining of the proteins. Thyroglobulin (TG) and protein(s) migrating more slowly than TG were present in all samples collected in vivo. A large number of samples also contained a fraction migrating at the front (prealbumin). An albuminlike protein was present in 2/3 of the samples and a protein fraction, migrating similarly to a tissue fluid protein, was observed in 1/3 of the samples. The 12S TG subunit was observed in a small number of colloid samples. Based on the presence of the different protein fractions in the colloid, the material was blocked into five qualitatively different groups. (Endocrinology 91: 1288, 1972)
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