Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
1984-3-23
pubmed:abstractText
A simple method for the isolation of bovine retinal S-antigen by ion-exchange chromatography on DEAE Sephadex, alone or in combination with a chromatafocusing step is described. High yields of highly purified S-antigen were obtained. Analytical studies indicated that the isolated protein was a single chain, 55 000 Mr glycoprotein with little tendency to self-association and a pI of 5.5. S-antigen prepared in the absence of protease inhibitors migrated on SDS-PAGE as a doublet but close similarity between both protein bands was observed by analysis of papain digests, suggesting that the protein was readily susceptible to proteolysis. S-antigen prepared by this method induces a selectively posterior focal uveoretinitis in a dose-dependent manner.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0014-4835
pubmed:author
pubmed:issnType
Print
pubmed:volume
37
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
613-25
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1983
pubmed:articleTitle
Purification of retinal S-antigen by ion-exchange chromatography and chromatofocusing.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't