Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1982-7-19
pubmed:abstractText
An unusual human cryoglobulin complex was characterized as a two-component system containing monoclonal immunoglobulin G (IgG) and serum albumin in a 1:2 mole ratio. This complex appeared to be an antibody-antigen complex, since the mole ratio was appropriate and the isolated Fab of the IgG associated with the albumin. The cryoglobulin apparently arose as a result of specific association and/or aggregation of the IgG albumin adduct, since the cryoglobulin complex formed a crystalline precipitate. The IgG and albumin were separated and characterized with respect to immunological cross-reactivities, sedimentation velocities, isoelectric properties, and amino acid composition. The extent of precipitation of the cryoglobulin complex was maximal at pH 7.8, was decreased by added ions including citrate, ethylenediaminetetraacetic acid, NaCl, and CaCl2, and was decreased by increasing temperature. Both the nature of the cold-precipitable complex and the solubility properties differed from those described for other cryoglobulins.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
19
pubmed:volume
21
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
289-94
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1982
pubmed:articleTitle
Characterization of a human cryoglobulin complex: a crystalline adduct of a monoclonal immunoglobulin G and albumin.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't