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rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:issue |
1
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|
pubmed:dateCreated |
1984-8-24
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|
pubmed:abstractText |
At moderate iodination levels (about 20 iodine atoms/mol) human thyroglobulin yields after reduction and alkylation a hormone (T4)-containing N-terminal peptide of 26K. Further iodination of the thyroglobulin in vitro results in the cleavage of this part of the molecule into smaller peptides of 22K and 18K. A precursor-product relationship between the 26K peptide segment and the latter was established by showing an identical N-terminal T4-containing sequence in the 3 peptides. Cleavage of peptide bonds in the 26K segment to give the smaller fragments could possibly be related to the formation of another hormone residue.
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pubmed:language |
fre
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pubmed:journal |
|
|
pubmed:citationSubset |
IM
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|
pubmed:chemical |
|
|
pubmed:status |
MEDLINE
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pubmed:issn |
0037-9026
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pubmed:author |
|
|
pubmed:issnType |
Print
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|
pubmed:volume |
178
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
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pubmed:pagination |
18-24
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|
pubmed:dateRevised |
2006-11-15
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|
pubmed:meshHeading |
|
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pubmed:year |
1984
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|
pubmed:articleTitle |
[Relation between the iodination of human thyroglobulin and the cleavage of the hormone peptide 26K N-terminal].
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|
pubmed:publicationType |
Journal Article,
English Abstract
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