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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
18
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pubmed:dateCreated |
1975-12-11
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pubmed:abstractText |
Thyroglobulin obtained from guinea pigs was examined by Na dodecyl-SO4-polyacrylamide gel electrophoresis after reduction and alkylation. In contrast to thyroglobulin from other mammalian sources, only three groups of polypeptide chains accounted for 95% or more of the protein. Determinations of the molecular weights of these purified proteins by equilibrium centrifugation in 6 M guanidine HCl gave values of 295,000 (species A), 210,000 (species B), and 110,000 (species C). Molecular weights determined by gel filtration in 6 M guanidine HCl gave similar results. Due to the large size of the polypeptides, satisfactory molecular weights could not be obtained from Na dodecyl-SO4-polyacrylamide gel electrophoresis. Amino acid analysis of the three species was similar to that of whole thyroglobulin. Only slightly higher level of lysine and histidine and a lower level of glutamic acid were seen in species C. The iodine contents were found to range from 0.07 to 0.12 to 0.20% for species A, B, and C, respectively.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
25
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pubmed:volume |
250
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pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
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pubmed:pagination |
7294-9
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pubmed:dateRevised |
2004-11-17
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pubmed:meshHeading |
pubmed-meshheading:1165242-Amino Acids,
pubmed-meshheading:1165242-Animals,
pubmed-meshheading:1165242-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:1165242-Guinea Pigs,
pubmed-meshheading:1165242-Iodine,
pubmed-meshheading:1165242-Macromolecular Substances,
pubmed-meshheading:1165242-Molecular Weight,
pubmed-meshheading:1165242-Thyroglobulin
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pubmed:year |
1975
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pubmed:articleTitle |
Elementary chain composition of guinea pig thyroglobulin.
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pubmed:publicationType |
Journal Article
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