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rdf:type |
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lifeskim:mentions |
umls-concept:C0019932,
umls-concept:C0030685,
umls-concept:C0040123,
umls-concept:C0080103,
umls-concept:C0086418,
umls-concept:C0391871,
umls-concept:C0542502,
umls-concept:C0680255,
umls-concept:C1283071,
umls-concept:C1515655,
umls-concept:C1533691,
umls-concept:C1963578
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pubmed:issue |
1
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pubmed:dateCreated |
1983-7-15
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pubmed:abstractText |
Reduced and S-alkylated thyroglobulin (Tgb) from different species were shown by SDS-PAGE to contain small peptides (from 45-9 kDa) rich in thyroxine. Several hypotheses were proposed to explain their origin. The polypeptide composition of iodine-poor (Tgb A) and normally iodinated (Tgb B) human Tgb prepared by two different procedures (one minimizing and the other favoring post-mortem proteolysis) was compared in the native state and after in vitro iodination. Results show that one of the hormonogenic sites of human Tgb is part of a domain of the molecule most susceptible to proteolysis, especially when it is very iodinated.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0014-5793
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pubmed:author |
|
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pubmed:issnType |
Print
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pubmed:day |
30
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pubmed:volume |
156
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
77-82
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pubmed:dateRevised |
2004-11-17
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pubmed:meshHeading |
pubmed-meshheading:6343118-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:6343118-Humans,
pubmed-meshheading:6343118-Iodine,
pubmed-meshheading:6343118-Peptide Fragments,
pubmed-meshheading:6343118-Peptide Hydrolases,
pubmed-meshheading:6343118-Protein Conformation,
pubmed-meshheading:6343118-Thyroglobulin,
pubmed-meshheading:6343118-Thyroid Hormones,
pubmed-meshheading:6343118-Thyroxine,
pubmed-meshheading:6343118-Tyrosine
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pubmed:year |
1983
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pubmed:articleTitle |
In vitro and in vivo iodination of human thyroglobulin in relation to hormone release.
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pubmed:publicationType |
Journal Article
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