|
rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:issue |
6
|
|
pubmed:dateCreated |
1997-2-6
|
|
pubmed:abstractText |
During the time course of disulfide bond formation by iodine oxidation (in a methanolic and hydrochloric acid solution) of a cysteinyl(S-acetamidomethyl)-glutaminyl tridecapeptide, we observed by ESI, FAB mass spectrometry (pseudo-molecular ion and ion-fragments) and 1H-NMR a side reaction due to a shift of the Acm leaving group from cysteine to the carboxamide side chain of glutamine. This type of Acm-shift at low level was described previously by L.W. Mendelson et al. (Int. J. Pept. Protein Res. 35:249-257) for an aspariginyl-cysteinyl(S-acetamidomethyl) peptide in an anhydrous hydrochloric solution. We report here the efficiency of glutamine as a scavenger to suppress the S-->N shift of the acetamidomethyl group during S-acetamidomethyl cleavage and sulfhydryl oxidation with iodine, as the folded tridecapeptide was obtained with the expected molecular weight.
|
|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
|
|
pubmed:status |
MEDLINE
|
|
pubmed:issn |
1040-5704
|
|
pubmed:author |
|
|
pubmed:issnType |
Print
|
|
pubmed:volume |
8
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
316-20
|
|
pubmed:dateRevised |
2006-11-15
|
|
pubmed:meshHeading |
pubmed-meshheading:8838414-Acetylcysteine,
pubmed-meshheading:8838414-Amino Acid Sequence,
pubmed-meshheading:8838414-Chromatography, High Pressure Liquid,
pubmed-meshheading:8838414-Disulfides,
pubmed-meshheading:8838414-Glutamine,
pubmed-meshheading:8838414-Iodine,
pubmed-meshheading:8838414-Kinetics,
pubmed-meshheading:8838414-Magnetic Resonance Spectroscopy,
pubmed-meshheading:8838414-Mass Spectrometry,
pubmed-meshheading:8838414-Molecular Sequence Data,
pubmed-meshheading:8838414-Molecular Weight,
pubmed-meshheading:8838414-Oxidation-Reduction,
pubmed-meshheading:8838414-Peptides
|
|
pubmed:articleTitle |
Side reaction of S-to-N acetamidomethyl shift during disulfide bond formation by iodine oxidation of S-acetamidomethyl-cysteine in a glutamine-containing peptide.
|
|
pubmed:affiliation |
CEA/Saclay, Gif sur Yvette, France.
|
|
pubmed:publicationType |
Journal Article
|
