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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
23
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pubmed:dateCreated |
1982-1-28
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pubmed:abstractText |
A general method for tritiating proteins, peptides, and other nonvolatile organic compounds has been developed. A carefully controlled particle beam composed of T3+ and T2+ ions and fast T2 molecules is accelerated into a sample target within a vacuum chamber. This beam method has been used to tritiate ribonuclease A, porcine pancreatic elastase, thermolysin, soybean trypsin inhibitor, alpha 1-protease inhibitor, and the peptide aldehydes leupeptin and antipain. After removal of all readily exchangeable tritium, the products were obtained in 32-83% yields with specific radioactivities of 18-856 Ci/mol. The products were carefully characterized, shown to be chemically pure, and to have complete biological activity. Simple tritium hydrogen exchange accounts for at least 82% of the reaction pathway with proteins and for 100% of the reaction with the peptide aldehydes. The ion beam method is a mild procedure for general tritium labeling of fragile protein macromolecules and other sensitive biological molecules.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Peptides,
http://linkedlifedata.com/resource/pubmed/chemical/Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Thermolysin,
http://linkedlifedata.com/resource/pubmed/chemical/Tritium,
http://linkedlifedata.com/resource/pubmed/chemical/Trypsin
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
|
pubmed:day |
10
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pubmed:volume |
256
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pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
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pubmed:pagination |
12213-21
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading | |
pubmed:year |
1981
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pubmed:articleTitle |
Ion beam tritium labeling of proteins and peptides.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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