Linked Life Data

2375232

Source:http://linkedlifedata.com/resource/pubmed/id/2375232

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
1990-8-24
pubmed:abstractText
IGFs were extracted from Cohn fraction IV of human plasma using ultrafiltration of acidified paste as the initial step. Further purification, including HPLC as the final steps, yielded seven IGF-like peptides: two with acidic pI (A1, A2), two with neutral pI (N1, N2), and three in the basic region (B1, B2 and B3). B1 was identified as IGF-I and N1 as IGF-II. The other peptides were further characterized with respect to their molecular weight and by N-terminal amino-acid sequencing. B2 and B3 are IGF-I-like, A1 and A2 and N2 are IGF-II-like. Two of the peptides (A2 and B3) appear to be two-chain forms of IGF-II and IGF-I, respectively, as shown by structural analysis and polyacrylamide gel electrophoresis. One peptide (A1) appears to be a new variant of an IGF-II derivative with a substitution of Ser by Cys in position 29. Further analysis involved reactivity in radioreceptor assays for IGF-I and IGF-II. N2, A1 and A2 are IGF-II-like, whereas B2 and B3 are IGF-I-like, though there are important differences with the main IGFs. Similar results were obtained in IGF-I and IGF-II C-peptide radioimmunoassays. The physiological significance of these peptides is unknown. They offer interesting perspectives for structure-function analysis.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0001-5598
pubmed:author
pubmed:issnType
Print
pubmed:volume
122
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
683-95
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1990
pubmed:articleTitle
Isolation and partial characterization of IGF-like peptides from Cohn fraction IV of human plasma.
pubmed:affiliation
University Hospital for Children and Youth, Het Wilhelmina Kinderziekenhuis, State University of Utrecht, The Netherlands.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't