Linked Life Data

2509567

Source:http://linkedlifedata.com/resource/pubmed/id/2509567

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1989-12-21
pubmed:abstractText
A culture of Streptococcus dysgalactiae (C 26) was shown to bind only to 125I-IgG, whereas another S. dysgalactiae culture (C 12) bound both 125I-IgG and 125I-albumin. The IgG-binding proteins could be readily solubilized by lysozyme treatment of the bacteria and isolated by affinity chromatography on IgG Sepharose. The purified IgG-binding protein from S. dysgalactiae C 26, which lacked simultaneous albumin binding activity, precipitated with IgG preparations from man, cow, horse, pig and mouse but not with chicken IgG. This IgG-binding protein was coupled to CNBr-activated Sepharose and subsequently used for the purification of IgG from both bovine and human serum. SDS-PAGE and immunoelectrophoretic studies confirmed the purity of the eluted proteins.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0022-1759
pubmed:author
pubmed:issnType
Print
pubmed:day
13
pubmed:volume
124
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
131-5
pubmed:dateRevised
2004-11-17
pubmed:meshHeading
pubmed:year
1989
pubmed:articleTitle
Isolation of immunoglobulin G by affinity chromatography using an IgG Fc receptor protein from Streptococcus dysgalactiae coupled to a solid phase.
pubmed:affiliation
Institut für Baketeriologie und Immunologie, Justus-Liebig-Universität, Giessen, F.R.G.
pubmed:publicationType
Journal Article