Linked Life Data

8120118

Source:http://linkedlifedata.com/resource/pubmed/id/8120118

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1994-4-5
pubmed:abstractText
Human serum immunoglobulin G was separated into its heavy and light chains by sodium dodecyl sulfate polyacrylamide gel electrophoresis and transferred electrophoretically to a polyvinylidenedifluoride membrane. Peptide fragments liberated from the light chain by in situ digestion with trypsin were then analyzed by reversed-phase high-performance liquid chromatography (HPLC). On comparing the HPLC patterns of these fragments derived from three major kappa marker (Km) types, two distinct peaks specific for the Km types were detected. Sequencing of the two specific peak peptides confirmed that they were identical to a stretch comprising residues 191-207 of the immunoglobulin kappa light chain, which contains valine/leucine allotypic variation at position 191.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0021-9673
pubmed:author
pubmed:issnType
Print
pubmed:day
8
pubmed:volume
622
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
9-12
pubmed:dateRevised
2005-11-17
pubmed:meshHeading
pubmed:year
1993
pubmed:articleTitle
Kappa marker typing with high-performance liquid chromatography: identification of kappa marker specific tryptic peptide from the kappa light chain of immunoglobulin G.
pubmed:affiliation
Department of Legal Medicine, Fukui Medical School, Japan.
pubmed:publicationType
Journal Article