Linked Life Data

7371974

Source:http://linkedlifedata.com/resource/pubmed/id/7371974

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1980-7-22
pubmed:abstractText
Previous electron-microscopical studies from this laboratory have shown that the thyroglobulin molecule can occur in two different conformations, one ovoid and the other cylindrical. Ovoid molecules are characteristic of well-iodinated thyroglobulin whereas cylindrical molecules are found after low-iodine diet or blocking of iodination. The present study was performed in order to elucidate the possible relation between the molecule conformation and the peroxidase-catalyzed reactions that occur in the thyroid in connection with hormone synthesis. Cylindrical thyroglobulin molecules (from PTU-exposed thyroids) were incubated in different media and the proportion of cylindrical and ovoid molecules after incubation was estimated in electron micrographs. It was found that incubation with glucose-glucose oxidase caused an extensive conversion of cylindrical molecules into ovoid molecules. Peroxidase and/or iodide were not necessary for this change of conformation. It is suggested that this in vitro molecule transformation was the result of an oxidation reaction.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0303-7207
pubmed:author
pubmed:issnType
Print
pubmed:volume
17
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
139-44
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1980
pubmed:articleTitle
Conformational change of the thyroglobulin molecule induced by oxidation in vitro.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.