Linked Life Data

6506025

Source:http://linkedlifedata.com/resource/pubmed/id/6506025

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
1985-1-10
pubmed:abstractText
A commercially available preparation of synthetic human fibrinopeptide B (FpB) was shown by hplc to contain two chromatographically distinct peaks, one of which was identical to FpB. Our results suggest that the contaminant peptide (FpB-2), which represented approximately 43% of the total peptide composition, is FpB containing an alpha-aminosuccinimide (Asc) residue. This Asc residue probably arose as a result of the cyclization of 5Asp-6Asn during either the coupling or deprotection reactions. FpB-2 was rapidly hydrolysed by carboxypeptidase B to des-Arg-FpB-2. It was stable under acidic conditions but in dilute alkali was converted to equimolar amounts of FpB and FpB containing beta-Asp at residue 5. Since it has been suggested that 5Asp-6Asn is a major immunorecognition site in FpB, our observations emphasize the need to establish the purity of synthetic FpB preparations destined for use in the immunoassay of either FpB or des-Arg-FpB.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0049-3848
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
35
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
697-702
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1984
pubmed:articleTitle
Peptide heterogeneity in a preparation of synthetic fibrinopeptide B.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't