rdf:type |
|
lifeskim:mentions |
umls-concept:C0001128,
umls-concept:C0021665,
umls-concept:C0034328,
umls-concept:C0035191,
umls-concept:C0037638,
umls-concept:C0082603,
umls-concept:C0220781,
umls-concept:C0596311,
umls-concept:C1330957,
umls-concept:C1883254,
umls-concept:C1948027
|
pubmed:issue |
4
|
pubmed:dateCreated |
1991-4-29
|
pubmed:abstractText |
Insulin-like growth factor I (IGF-I), a protein of 70 amino acid residues and 3 cystine bridges, has been synthesized by two solid phase Boc methods. The first method used N-methylpyrrolidinone as the solvent with single coupling cycles while the second synthesis used dimethylformamide and dichloromethane as the solvents with a double-coupling protocol. In both cases, trifluoroacetic acid/trifluoromethanesulphonic acid cleavage of the peptide from the resin was employed. Purification of the cleavage products followed by removal of the S-acetamidomethyl protecting groups gave reduced peptides which were then oxidized under conditions favouring the formation of the correct disulphide bonds. The purified synthetic IGF-I peptides were full agonists of natural IGF-I in a radioimmunoassay, in an IGF-I radioreceptor assay, in a bioassay which measures the stimulation of protein synthesis in rat L6 myoblasts and in an IGF-binding protein competitive binding assay. Moreover, in each of these assays, the synthetic IGF peptides were found to be at least 70% as potent as natural IGF-I.
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pubmed:language |
eng
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pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/1-methyl-2-pyrrolidinone,
http://linkedlifedata.com/resource/pubmed/chemical/Indicators and Reagents,
http://linkedlifedata.com/resource/pubmed/chemical/Insulin-Like Growth Factor I,
http://linkedlifedata.com/resource/pubmed/chemical/Mesylates,
http://linkedlifedata.com/resource/pubmed/chemical/Pyrrolidinones,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Cell Surface,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Somatomedin,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Resins, Plant,
http://linkedlifedata.com/resource/pubmed/chemical/Solvents,
http://linkedlifedata.com/resource/pubmed/chemical/trifluoromethanesulfonic acid
|
pubmed:status |
MEDLINE
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pubmed:month |
Oct
|
pubmed:issn |
0367-8377
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pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:volume |
36
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
356-61
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:1964154-Animals,
pubmed-meshheading:1964154-Binding, Competitive,
pubmed-meshheading:1964154-Cell Line,
pubmed-meshheading:1964154-Cell Membrane,
pubmed-meshheading:1964154-Chromatography, High Pressure Liquid,
pubmed-meshheading:1964154-Humans,
pubmed-meshheading:1964154-Indicators and Reagents,
pubmed-meshheading:1964154-Insulin-Like Growth Factor I,
pubmed-meshheading:1964154-Mesylates,
pubmed-meshheading:1964154-Pyrrolidinones,
pubmed-meshheading:1964154-Receptors, Cell Surface,
pubmed-meshheading:1964154-Receptors, Somatomedin,
pubmed-meshheading:1964154-Recombinant Proteins,
pubmed-meshheading:1964154-Resins, Plant,
pubmed-meshheading:1964154-Solvents
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pubmed:year |
1990
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pubmed:articleTitle |
Synthesis of insulin-like growth factor I using N-methyl pyrrolidinone as the coupling solvent and trifluoromethane sulphonic acid cleavage from the resin.
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pubmed:affiliation |
Biochemistry Department, University of Adelaide, SA.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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