Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1989-2-22
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).
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0013-7219
pubmed:author
pubmed:issnType
Print
pubmed:volume
35
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
275-83
pubmed:dateRevised
2004-9-20
pubmed:meshHeading
pubmed:year
1988
pubmed:articleTitle
Purification of TSH receptor from porcine thyroid membrane and effect of various protease inhibitors on receptor stability.
pubmed:affiliation
Department of Medicine, Kyoto University Faculty of Medicine, Japan.
pubmed:publicationType
Journal Article