Abstract
ABSTRACT Distribution of protein and I131 in centrifugally fractionated thyroid homogenates, and the electrophoretic, solubility and ultracentrifuge characteristics of the soluble fraction were studied in normal and diseased human thyroid glands. In the normal glands, 64–82 per cent of the protein and 95 per cent of the I131-label appeared in the soluble fraction. Thyroglobulin comprised 70–79 per cent of the soluble protein. Normal thyroglobulin had a Svedberg constant (0.5 per cent solution in 0.9 per cent NaCl) of 18–20, and salted out of phosphate buffer at 1.7–1.9 M. No protein with greater mobility than thyroglobulin was detected on paper electrophoresis in barbital buffer. In all diseased glands, an increased proportion of light-weight (Sw.20 = 4) protein was observed, and the thyroglobulin usually had greater solubility in phosphate buffer. In the soluble fraction of some colloid goiters, 1 follicular adenoma, 3 congenital goiters and 1 thyroid carcinoma, a protein as yet indistinguishable from al...
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