Linked Life Data

2076469

Source:http://linkedlifedata.com/resource/pubmed/id/2076469

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
11
pubmed:dateCreated
1991-4-22
pubmed:abstractText
Disulphide bridges have been assigned in three different proteins by locating possible disulphide-linked peptides in enzymic digests of the proteins based on their molecular weight determined by plasma desorption mass spectrometry. Different strategies have been employed including in situ reduction of the nitrocellulose-bound peptides and confirmation of peptide identity by methyl esterification reactions or Edman degradation. The latter was needed for identification of glycosylated disulphide-linked peptides. For insulins cleavage between cysteine residues in close proximity was not possible; but a combination of molecular mass information, enzymic cleavage with two different enzymes and sequence analysis including identification of di-phenylthiohydantoin-cystine could ensure an unambiguous assignment of the disulphide bridges.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0887-6134
pubmed:author
pubmed:issnType
Print
pubmed:volume
19
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
713-20
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed:year
1990
pubmed:articleTitle
Strategies for determination of disulphide bridges in proteins using plasma desorption mass spectrometry.
pubmed:affiliation
Novo Nordisk a/s, Niels Steensensvej 1, Gentofte, Denmark.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't