Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1989-2-16
pubmed:abstractText
Soluble immune response suppressor (SIRS) is an immunosuppressive protein which requires activation to SIRSox by peroxide. This observation suggested that SIRS could be a metalloprotein. To investigate this possibility, purified hybridoma-derived SIRS was treated with chelating agents and dialyzed prior to activation with H2O2. EDTA, EGTA, or desferrioxamine prevented suppression of murine plaque-forming cell responses by SIRSox, whereas sodium citrate and penicillamine did not inhibit suppression. Suppressive activity was reconstituted by subsequent treatment of SIRS with FeSO4 (0.5 microM), NiSO4 (500 microM), or MgSO4 (500 microM), but not by FeCl3, MnSO4, CuSO4, ZnSO4, CaCl2, or CrCl3. Reconstitution of activity occurred only if FeSO4 was added at least 3 hr prior to treatment with H2O2. These data indicate that SIRS requires a divalent metal ion, probably ferrous iron, for activity, and suggest that SIRS is a metalloprotein.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0008-8749
pubmed:author
pubmed:issnType
Print
pubmed:volume
118
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
157-65
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1989
pubmed:articleTitle
Divalent metal requirement for soluble immune response suppressor (SIRS) activity.
pubmed:affiliation
Department of Pathology, Jewish Hospital, St. Louis, Missouri 63110.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't