| pubmed-article:3061781 | pubmed:abstractText | Purification of porcine thyroid TSH receptors was attempted by using Lubrol, TSH-Sepharose, gel filtration and the immunoabsorption by anti-thyroglobulin (Tg) antibody-Sepharose. The effects of microbial protease inhibitors on the degradation of TSH receptors were also evaluated. Porcine thyroid membrane was solubilized with 1% Lubrol-PX and TSH receptors were purified by TSH affinity chromatography, followed by gel filtration on TSKgel-G3000SW. A partial purification was achieved; a 692-fold purification and 49.3% recovery of high affinity binding site and a 409-fold purification and 29.1% recovery of low affinity binding site, respectively. Rechromatography on G3000SW gel and immunoabsorption by anti-Tg antibody-Sepharose resulted in further reduction of contaminants. Among 10 protease inhibitors studied, a low concentration of chymostatin was the only one that showed a significant protective effect on the degradation of the receptors (p less than 0.05). | lld:pubmed |
