Solubilization, purification, and partial characterization of thyrotropin receptor from bovine and human thyroid glands.

Abstract:

:In an attempt to purify the thyroid receptor for TSH and to study interaction with the thyroid-stimulating antibody (TSAb) of graves' disease, we used both bovine and human thyroid glands. With either tissue, the 10,000 X g pellet of homogenized material was solubilized with 0.5% Triton N-101; excess Triton was removed by Amberlite XAD-2, and purification was effected by TSH affinity chromatography, followed by gel filtration on Sepharose 6B. Greatest purification was achieved with bovine tissue; this receptor preparation was 183-fold concentrated over the starting material, but contained only 6% of the original TSH-binding activity, due in part to spontaneous loss over the 4 days required for processing. On polyacrylamide gel electrophoresis, there were at least three protein bands, one of which was probably a subunit of thyroglobulin. Purified immunoglobulin G with thyroid-stimulating antibody activity inhibited the binding of TSH at all stages of purification of the receptor.

journal_name

Endocrinology

journal_title

Endocrinology

authors

Koizumi Y,Zakarija M,McKenzie JM

doi

10.1210/endo-110-4-1381

subject

Has Abstract

pub_date

1982-04-01 00:00:00

pages

1381-91

issue

4

eissn

0013-7227

issn

1945-7170

journal_volume

110

pub_type

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