Linked Life Data

2495325

Source:http://linkedlifedata.com/resource/pubmed/id/2495325

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
8
pubmed:dateCreated
1989-5-22
pubmed:abstractText
Staphylococcal protein A (SPA) is a bacterial membrane protein which has distinct binding sites for Fc gamma and for the Fab region of some IgM, IgG, IgA, and IgE molecules. This study establishes a structure-function correlation responsible for the binding of Ig Fab regions to SPA. Binding of 24 isolated human monoclonal IgM proteins to SPA was measured in a solid phase RIA. VH and V kappa subgroups of each IgM were determined by SDS-PAGE, transfer blotting, and detection with antisera prepared against specific first framework region peptides. Binding to SPA was seen with 10 of 11 VHIII IgM, but none of the 7 VHI or 6 VHII. Similarly, polyclonal IgM fractionated on a SPA-Sepharose CL4B column showed nearly complete partition of VHIII molecules into the SPA-binding fraction, and VHI and VHII subgroup proteins into the fall-through. We conclude that SPA binding is a functional marker for VHIII H chains in human IgM molecules.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
AIM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0022-1767
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
142
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2778-83
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1989
pubmed:articleTitle
Human IgM molecules that bind staphylococcal protein A contain VHIII H chains.
pubmed:affiliation
Department of Medicine, University of Washington, Seattle 98195.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't